|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-203 |
5.47e-118 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 333.31 E-value: 5.47e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIG 82
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 83 HQPGIKTRLTALENLHFYHR---DGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAI 159
Cdd:PRK13538 81 HQPGIKTELTALENLRFYQRlhgPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 9911057 160 DVNGVDRLTQRMAQHTEQGGIVILTTHQPLNVAESKIRRISLTQ 203
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRLGQ 204
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-204 |
2.64e-108 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 309.04 E-value: 2.64e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 4 LEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGH 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 84 QPGIKTRLTALENLHFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNG 163
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9911057 164 VDRLTQRMAQHTEQGGIVILTTHQPLNVAESKIRRISLTQT 204
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLGFK 201
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-199 |
2.55e-96 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 278.47 E-value: 2.55e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 4 LEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGH 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 84 QPGIKTRLTALENLHFYHRDGDTAQ--CLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDV 161
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQrtIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 9911057 162 NGVDRLTQRMAQHTEQGGIVILTTHQPLNVAESKIRRI 199
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHQDLGLVEARELRL 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-205 |
5.18e-88 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 257.79 E-value: 5.18e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIG 82
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 83 HQPGIKTRLTALENLHFYHR----DGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTA 158
Cdd:COG4133 82 HADGLKPELTVRENLRFWAAlyglRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 9911057 159 IDVNGVDRLTQRMAQHTEQGGIVILTTHQPLNVAEskIRRISLTQTR 205
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA--ARVLDLGDFK 206
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-199 |
2.17e-57 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 180.07 E-value: 2.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLH--QVRDSYHqnllW 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdpDVAEACH----Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 81 IGHQPGIKTRLTALENLHFYH--RDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTA 158
Cdd:PRK13539 78 LGHRNAMKPALTVAENLEFWAafLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9911057 159 IDVNGVDRLTQRMAQHTEQGGIVILTTHQPLNVAESKIRRI 199
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAATHIPLGLPGARELDL 198
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-193 |
1.60e-39 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 134.31 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIG 82
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 83 HQPGIKTRLTALENLHF-YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDV 161
Cdd:PRK13540 81 HRSGINPYLTLRENCLYdIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|....
gi 9911057 162 NGVDRLTQRMAQHTEQGGIVILTTHQ--PLNVAE 193
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSHQdlPLNKAD 194
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-186 |
9.53e-39 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 132.67 E-value: 9.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHqnLLWIG 82
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRF--MAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 83 HQPGIKTRLTALENLHFYHR-DGDTAQCL--EALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAI 159
Cdd:PRK13543 89 HLPGLKADLSTLENLHFLCGlHGRRAKQMpgSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
170 180
....*....|....*....|....*..
gi 9911057 160 DVNGVDRLTQRMAQHTEQGGIVILTTH 186
Cdd:PRK13543 169 DLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-157 |
1.76e-33 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 116.98 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 19 FSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLH-QVRDSYHQNLLWIGHQPGIKTRLTALENL 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 98 ------HFYHRDGDTAQCLEALAQAGLAGFEDIPV----NQLSAGQQRRVALARLWLTRATLWILDEPFT 157
Cdd:pfam00005 81 rlglllKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-188 |
1.14e-32 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 117.65 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIG 82
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 83 HQPGIKTRLTALENLHFY------HRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPF 156
Cdd:COG4555 81 DERGLYDRLTVRENIRYFaelyglFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190
....*....|....*....|....*....|..
gi 9911057 157 TAIDVNGVDRLTQRMAQHTEQGGIVILTTHQP 188
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIM 192
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
21-199 |
1.86e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 111.69 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQPGIKTRLTALENLHFY 100
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQEPALYPDLTVRENLRFF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 101 ------HRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQH 174
Cdd:COG1131 98 arlyglPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLREL 177
|
170 180
....*....|....*....|....*
gi 9911057 175 TEQGGIVILTTHQpLNVAESKIRRI 199
Cdd:COG1131 178 AAEGKTVLLSTHY-LEEAERLCDRV 201
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-186 |
2.91e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 111.33 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 1 MGMLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHQV 70
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGK----------StllkailgllPPTSGTVRLFGKPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 71 RD--SY---HQNLLWigHQPgiktrLTALE--NLHFYHRDG--------DTAQCLEALAQAGLAGFEDIPVNQLSAGQQR 135
Cdd:COG1121 74 RRriGYvpqRAEVDW--DFP-----ITVRDvvLMGRYGRRGlfrrpsraDREAVDEALERVGLEDLADRPIGELSGGQQQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9911057 136 RVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTH 186
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTH 197
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-193 |
1.32e-27 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 109.08 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQV-RDSYHQNLLWIGHQPGIkTRLT 92
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLdPASWRRQIAWVPQNPYL-FAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 93 ALENLHFYHRDGDTAQCLEALAQAGLAGFedipVNQ---------------LSAGQQRRVALARLWLTRATLWILDEPFT 157
Cdd:COG4988 427 IRENLRLGRPDASDEELEAALEAAGLDEF----VAAlpdgldtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
170 180 190
....*....|....*....|....*....|....*.
gi 9911057 158 AIDVNGVDRLTQRMAQHTeQGGIVILTTHQPLNVAE 193
Cdd:COG4988 503 HLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ 537
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-205 |
1.09e-26 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 99.63 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 5 EARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIghq 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 85 pgiktrltalenlhfyhrdgdtaqclealaqaglagfedipVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGV 164
Cdd:cd00267 78 -----------------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9911057 165 DRLTQRMAQHTEQGGIVILTTHQPLNVAESKIRRISLTQTR 205
Cdd:cd00267 117 ERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
21-199 |
3.67e-24 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 93.62 E-value: 3.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQPGIKTR 90
Cdd:cd03230 18 DISLTVEKGEIYGLLGPNGAGK----------TtlikiilgllKPDSGEIKVLGKDIKKEPEEVKRRIGYLPEEPSLYEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 LTALENLHfyhrdgdtaqclealaqaglagfedipvnqLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQR 170
Cdd:cd03230 88 LTVRENLK------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWEL 137
|
170 180
....*....|....*....|....*....
gi 9911057 171 MAQHTEQGGIVILTTHQpLNVAESKIRRI 199
Cdd:cd03230 138 LRELKKEGKTILLSSHI-LEEAERLCDRV 165
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
3-199 |
9.75e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 93.40 E-value: 9.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSgLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYhqnLLWIG 82
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY---CTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 83 HQPGIKTRLTALENLHFYHRDGDTAQCLEA-LAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDV 161
Cdd:PRK13541 77 HNLGLKLEMTVFENLKFWSEIYNSAETLYAaIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 9911057 162 NGVDRLTQRMAQHTEQGGIVILTTHQPLNVAESKIRRI 199
Cdd:PRK13541 157 ENRDLLNNLIVMKANSGGIVLLSSHLESSIKSAQILQL 194
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-186 |
1.47e-23 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 92.98 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDsyhqnllWIGHQPGIKT---- 89
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-------RIGYVPQRRSidrd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 90 -RLTALE----------NLHFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTA 158
Cdd:cd03235 83 fPISVRDvvlmglyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180
....*....|....*....|....*...
gi 9911057 159 IDVNGVDRLTQRMAQHTEQGGIVILTTH 186
Cdd:cd03235 163 VDPKTQEDIYELLRELRREGMTILVVTH 190
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
15-188 |
3.67e-23 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 96.37 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQV-RDSYHQNLLWIGHQPGI-KTrlT 92
Cdd:COG4987 347 GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLdEDDLRRRIAVVPQRPHLfDT--T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 93 ALENLHFYHRDGDTAQCLEALAQAGLAGF-EDIPVN----------QLSAGQQRRVALARLWLTRATLWILDEPFTAIDV 161
Cdd:COG4987 425 LRENLRLARPDATDEELWAALERVGLGDWlAALPDGldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDA 504
|
170 180
....*....|....*....|....*..
gi 9911057 162 NGVDRLTQRMAQHTeQGGIVILTTHQP 188
Cdd:COG4987 505 ATEQALLADLLEAL-AGRTVLLITHRL 530
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-192 |
1.16e-22 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 91.64 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHqvrdSYH-----QN 77
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA----SLSrrelaRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 78 LLWIGHQPGIKTRLTALE----------NLHFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRA 147
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRElvalgryphlGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9911057 148 TLWILDEPFTAIDVN---GVDRLTQRMAQhtEQGGIVILTTHQpLNVA 192
Cdd:COG1120 157 PLLLLDEPTSHLDLAhqlEVLELLRRLAR--ERGRTVVMVLHD-LNLA 201
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-193 |
1.54e-22 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 90.85 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQP-----LHQVRDSyhqnl 78
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGK----------StllrllngllKPTSGEVLVDGKDitkknLRELRRK----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 79 lwIG-------HQpgiktrLTA----------LENLHFyhrDGDTAQ--CLEALAQAGLAGFEDIPVNQLSAGQQRRVAL 139
Cdd:COG1122 77 --VGlvfqnpdDQ------LFAptveedvafgPENLGL---PREEIRerVEEALELVGLEHLADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9911057 140 ARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQPLNVAE 193
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAE 199
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-188 |
2.78e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 93.51 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 13 RDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPL-HQVRDSYHQNLLWIGHQPGIkTRL 91
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLaDADADSWRDQIAWVPQHPFL-FAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 TALENLHFYHRDGDTAQCLEALAQAGLAGF-EDIPV----------NQLSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:TIGR02857 411 TIAENIRLARPDASDAEIREALERAGLDEFvAALPQgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180
....*....|....*....|....*...
gi 9911057 161 VNGVDRLTQRMAQHTeQGGIVILTTHQP 188
Cdd:TIGR02857 491 AETEAEVLEALRALA-QGRTVLLVTHRL 517
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-187 |
6.43e-22 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 88.68 E-value: 6.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 12 ERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQvrDSYHQNLLWIG-------HQ 84
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK--LSLKELRRKVGlvfqnpdDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 85 PgIKTRLT-----ALENLHFYHRDGDTAQcLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAI 159
Cdd:cd03225 88 F-FGPTVEeevafGLENLGLPEEEIEERV-EEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180
....*....|....*....|....*...
gi 9911057 160 DVNGVDRLTQRMAQHTEQGGIVILTTHQ 187
Cdd:cd03225 166 DPAGRRELLELLKKLKAEGKTIIIVTHD 193
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-192 |
1.21e-21 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 87.11 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 5 EARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVrdSYHQNLLWIGHQ 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL--SPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 85 PgiktrltalenlhfyhrdgdtaQCLEALaqaGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGV 164
Cdd:cd03214 79 P----------------------QALELL---GLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180
....*....|....*....|....*....
gi 9911057 165 DRLTQRMAQHTEQGGI-VILTTHQpLNVA 192
Cdd:cd03214 134 IELLELLRRLARERGKtVVMVLHD-LNLA 161
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
15-187 |
9.90e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 85.80 E-value: 9.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLhqvrDSYHQNLlwIGHQP---GIKTRL 91
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNR--IGYLPeerGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 TALENLHFY-------HRDGdTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGV 164
Cdd:cd03269 86 KVIDQLVYLaqlkglkKEEA-RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180
....*....|....*....|...
gi 9911057 165 DRLTQRMAQHTEQGGIVILTTHQ 187
Cdd:cd03269 165 ELLKDVIRELARAGKTVILSTHQ 187
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-188 |
4.14e-20 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 84.11 E-value: 4.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQV----RDsyhqnllwIG---HQPG 86
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVpperRN--------IGmvfQDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 87 IKTRLTALENLHF--YHRDGDTAQ----CLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:cd03259 83 LFPHLTVAENIAFglKLRGVPKAEirarVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180
....*....|....*....|....*....
gi 9911057 161 VNGVDRLTQRMAQ-HTEQGGIVILTTHQP 188
Cdd:cd03259 163 AKLREELREELKElQRELGITTIYVTHDQ 191
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-188 |
1.30e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 83.27 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTL-FSglsFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHQVr 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPLrFD---LTIAAGERVAILGPSGAGK----------StllnliagflPPDSGRILWNGQDLTAL- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 72 dSYHQ----------NLLWigHqpgiktrLTALENLHFYHRDG------DTAQCLEALAQAGLAGFEDIPVNQLSAGQQR 135
Cdd:COG3840 67 -PPAErpvsmlfqenNLFP--H-------LTVAQNIGLGLRPGlkltaeQRAQVEQALERVGLAGLLDRLPGQLSGGQRQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9911057 136 RVALARLWLTRATLWILDEPFTAIDVNgvdrLTQRMAQ-----HTEQGGIVILTTHQP 188
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPA----LRQEMLDlvdelCRERGLTVLMVTHDP 190
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
21-201 |
1.44e-19 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 82.92 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDS-----YHQNLLWIGHQPGIKTRLTALE 95
Cdd:cd03255 22 GVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafRRRHIGFVFQSFNLLPDLTALE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 96 N----LHFYHRDGDTA--QCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAID-VNG--VDR 166
Cdd:cd03255 102 NvelpLLLAGVPKKERreRAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDsETGkeVME 181
|
170 180 190
....*....|....*....|....*....|....*
gi 9911057 167 LTQRMAQhtEQGGIVILTTHQPlNVAESKIRRISL 201
Cdd:cd03255 182 LLRELNK--EAGTTIVVVTHDP-ELAEYADRIIEL 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-188 |
3.91e-19 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 82.23 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRD----SYHQNLLWIGHQPGIKT 89
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrQLRRQIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 90 RLTALEN---------------LHFYHRDgDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDE 154
Cdd:cd03256 92 RLSVLENvlsgrlgrrstwrslFGLFPKE-EKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190
....*....|....*....|....*....|....*
gi 9911057 155 PFTAIDVNGVDRLTQRMAQ-HTEQGGIVILTTHQP 188
Cdd:cd03256 171 PVASLDPASSRQVMDLLKRiNREEGITVIVSLHQV 205
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-188 |
4.79e-19 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 82.03 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCE-RDERTLFSGLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHQVR 71
Cdd:COG3638 2 MLELRNLSKRyPGGTPALDDVSLEIERGEFVALIGPSGAGK----------StllrclnglvEPTSGEILVDGQDVTALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 72 DSY-----------HQnllwighQPGIKTRLTALEN---------------LHFYHRDgDTAQCLEALAQAGLAGFEDIP 125
Cdd:COG3638 72 GRAlrrlrrrigmiFQ-------QFNLVPRLSVLTNvlagrlgrtstwrslLGLFPPE-DRERALEALERVGLADKAYQR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9911057 126 VNQLSAGQQRRVALARLWLTRATLWILDEPFTAID-VNGVD--RLTQRMAQhtEQGGIVILTTHQP 188
Cdd:COG3638 144 ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDpKTARQvmDLLRRIAR--EDGITVVVNLHQV 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
12-193 |
6.12e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 82.06 E-value: 6.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 12 ERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSY---HQN--LL-Wighqp 85
Cdd:COG1116 20 GGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRgvvFQEpaLLpW----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 86 giktrLTALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAI 159
Cdd:COG1116 95 -----LTVLDNVALglelrgVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9911057 160 DVngvdrLTQRMAQ------HTEQGGIVILTTHqplNVAE 193
Cdd:COG1116 170 DA-----LTRERLQdellrlWQETGKTVLFVTH---DVDE 201
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-188 |
6.21e-19 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 84.12 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQV-RDSYHQNllwIGH--QpgiKTR 90
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIdPASLRRQ---IGVvlQ---DVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 L---TALENLHFYHRDGDTAQCLEALAQAGLAGF-------EDIPV----NQLSAGQQRRVALARLWLTRATLWILDEPF 156
Cdd:COG2274 560 LfsgTIRENITLGDPDATDEEIIEAARLAGLHDFiealpmgYDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
170 180 190
....*....|....*....|....*....|..
gi 9911057 157 TAIDVNGVDRLTQRMAQHTeQGGIVILTTHQP 188
Cdd:COG2274 640 SALDAETEAIILENLRRLL-KGRTVIIIAHRL 670
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-186 |
3.71e-18 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 78.95 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQPGIKTRLTALENLHFY 100
Cdd:cd03266 23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGLYDRLTARENLEYF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 101 ------HRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQH 174
Cdd:cd03266 103 aglyglKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL 182
|
170
....*....|..
gi 9911057 175 TEQGGIVILTTH 186
Cdd:cd03266 183 RALGKCILFSTH 194
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
15-186 |
4.48e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 78.93 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRD----------------SYhqNL 78
Cdd:COG1136 20 EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelarlrrrhigfvfqFF--NL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 79 LwighqPgiktRLTALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWIL 152
Cdd:COG1136 98 L-----P----ELTALENVALplllagVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILA 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 9911057 153 DEPFTAID-VNGVD--RLTQRMAQhtEQGGIVILTTH 186
Cdd:COG1136 169 DEPTGNLDsKTGEEvlELLRELNR--ELGTTIVMVTH 203
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-161 |
6.63e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 79.08 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEAREL----LCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRD-SYHQN 77
Cdd:COG1124 1 MLEVRNLsvsyGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 78 LLWIGHQP--------GIKTRLTalENLHFYHRDGDTAQCLEALAQAGL-AGFEDIPVNQLSAGQQRRVALARLWLTRAT 148
Cdd:COG1124 81 VQMVFQDPyaslhprhTVDRILA--EPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170
....*....|...
gi 9911057 149 LWILDEPFTAIDV 161
Cdd:COG1124 159 LLLLDEPTSALDV 171
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-186 |
7.30e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.35 E-value: 7.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTL-FSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSyhqnLLWI 81
Cdd:PRK13639 1 ILETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKS----LLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 82 GHQPGI-----KTRL---TALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRA 147
Cdd:PRK13639 77 RKTVGIvfqnpDDQLfapTVEEDVAFgplnlgLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 9911057 148 TLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTH 186
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-201 |
3.33e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 76.63 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 13 RDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSY-----------HQN--LL 79
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrrrigvvFQDfrLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 80 wighqpgikTRLTALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILD 153
Cdd:COG2884 92 ---------PDRTVYENVALplrvtgKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9911057 154 EPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQPLNVAESKIRRISL 201
Cdd:COG2884 163 EPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLEL 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-187 |
1.17e-16 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 75.23 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 13 RDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNL-LWIG---HQPGIK 88
Cdd:cd03261 10 FGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrRRMGmlfQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 89 TRLTALENLHF---YHRDGD----TAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAID- 160
Cdd:cd03261 90 DSLTVFENVAFplrEHTRLSeeeiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDp 169
|
170 180
....*....|....*....|....*....
gi 9911057 161 --VNGVDRLTQRMAQhtEQGGIVILTTHQ 187
Cdd:cd03261 170 iaSGVIDDLIRSLKK--ELGLTSIMVTHD 196
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-201 |
1.20e-16 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 74.75 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDS----YHQNLLWIGHQPGIKTRLTALE 95
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipyLRRKIGVVFQDFRLLPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 96 NLHF-----YHRDGDTAQ-CLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQ 169
Cdd:cd03292 98 NVAFalevtGVPPREIRKrVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMN 177
|
170 180 190
....*....|....*....|....*....|..
gi 9911057 170 RMAQHTEQGGIVILTTHQPLNVAESKIRRISL 201
Cdd:cd03292 178 LLKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-188 |
1.27e-16 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 75.02 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 23 SFTLNA-----GEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYH------------QNLLWIGHqp 85
Cdd:cd03297 12 DFTLKIdfdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlppqqrkiglvfQQYALFPH-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 86 giktrLTALENLHF---YHRDGDTAQCLEALAQA-GLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDV 161
Cdd:cd03297 90 -----LNVRENLAFglkRKRNREDRISVDELLDLlGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180
....*....|....*....|....*...
gi 9911057 162 NGVDRLTQRMAQ-HTEQGGIVILTTHQP 188
Cdd:cd03297 165 ALRLQLLPELKQiKKNLNIPVIFVTHDL 192
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-186 |
1.58e-16 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 75.02 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHQVRD 72
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGK----------SvllkliigllRPDSGEILVDGQDITGLSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 73 SYHQNL------------LWighqpgikTRLTALENLHF---YHRDGDTAQC----LEALAQAGLAGFEDIPVNQLSAGQ 133
Cdd:COG1127 75 KELYELrrrigmlfqggaLF--------DSLTVFENVAFplrEHTDLSEAEIrelvLEKLELVGLPGAADKMPSELSGGM 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9911057 134 QRRVALARLWLTRATLWILDEPFTAID---VNGVDRLTQRMaqHTEQGGIVILTTH 186
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDpitSAVIDELIREL--RDELGLTSVVVTH 200
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-188 |
2.20e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 76.63 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 19 FSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVR-DSYHQNLLWIGHQPGIKTRlTALENL 97
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqDEVRRRVSVCAQDAHLFDT-TVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 98 HFYHRDGDTAQCLEALAQAGLA-------GFEDIPVNQ----LSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDR 166
Cdd:TIGR02868 430 RLARPDATDEELWAALERVGLAdwlralpDGLDTVLGEggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
170 180
....*....|....*....|..
gi 9911057 167 LTQRMAQhTEQGGIVILTTHQP 188
Cdd:TIGR02868 510 LLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
19-186 |
4.86e-16 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 73.38 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 19 FSGLSFTLNAGEWVqITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQPGIKTRLTALENLH 98
Cdd:cd03264 16 LDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQEFGVYPNFTVREFLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 99 FY-------HRDGDtAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDV---NGVDRLT 168
Cdd:cd03264 95 YIawlkgipSKEVK-ARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPeerIRFRNLL 173
|
170
....*....|....*...
gi 9911057 169 QRMAQHTeqggIVILTTH 186
Cdd:cd03264 174 SELGEDR----IVILSTH 187
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-188 |
5.37e-16 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 73.58 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 13 RDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLW-QGQPLHQVRdsyhqnlLW-----IGH--- 83
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlFGERRGGED-------VWelrkrIGLvsp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 84 --QPGIKTRLTALE--------NLHFYHR--DGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWI 151
Cdd:COG1119 86 alQLRFPRDETVLDvvlsgffdSIGLYREptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 9911057 152 LDEPFTAIDVNGVDRLTQRMAQHTEQGGI-VILTTHQP 188
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLAAEGAPtLVLVTHHV 203
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
21-187 |
5.74e-16 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 73.49 E-value: 5.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRD----SYHQNLLWIGHQPGIKTRLTALEN 96
Cdd:TIGR02315 20 NINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkklrKLRRRIGMIFQHYNLIERLTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 97 ---------------LHFYHRDgDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAID- 160
Cdd:TIGR02315 100 vlhgrlgykptwrslLGRFSEE-DKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDp 178
|
170 180
....*....|....*....|....*....
gi 9911057 161 --VNGVDRLTQRMAQhtEQGGIVILTTHQ 187
Cdd:TIGR02315 179 ktSKQVMDYLKRINK--EDGITVIINLHQ 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-186 |
5.82e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.87 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPL-HQVRDSYHQnllwIGHQP---GIKTRLTALE 95
Cdd:PRK13536 58 NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLARAR----IGVVPqfdNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 96 NLHFYHRD-GDTAQCLEA-----LAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQ 169
Cdd:PRK13536 134 NLLVFGRYfGMSTREIEAvipslLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWE 213
|
170
....*....|....*..
gi 9911057 170 RMAQHTEQGGIVILTTH 186
Cdd:PRK13536 214 RLRSLLARGKTILLTTH 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
15-187 |
6.44e-16 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 72.63 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQnllwIG---HQPGIKTRL 91
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR----IGaliEAPGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 TALENLHFYHR--DGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQ 169
Cdd:cd03268 88 TARENLRLLARllGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRE 167
|
170
....*....|....*...
gi 9911057 170 RMAQHTEQGGIVILTTHQ 187
Cdd:cd03268 168 LILSLRDQGITVLISSHL 185
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-191 |
7.73e-16 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 71.65 E-value: 7.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHQV-RDSYHQNLLWIG 82
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGK----------StllklllrlyDPTSGEILIDGVDLRDLdLESLRKNIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 83 HQPGIKTRlTALENLhfyhrdgdtaqclealaqaglagfedipvnqLSAGQQRRVALARLWLTRATLWILDEPFTAIDVN 162
Cdd:cd03228 83 QDPFLFSG-TIRENI-------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180
....*....|....*....|....*....
gi 9911057 163 GVDRLTQRMAQHTeQGGIVILTTHQPLNV 191
Cdd:cd03228 131 TEALILEALRALA-KGKTVIVIAHRLSTI 158
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-192 |
8.11e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.88 E-value: 8.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 1 MGMLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLH---------QVR 71
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalsaraasrRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 72 ----------DSYHQNLLWIGHQPGiKTRLTAlenlhfyHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALAR 141
Cdd:PRK09536 81 svpqdtslsfEFDVRQVVEMGRTPH-RSRFDT-------WTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9911057 142 LWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQpLNVA 192
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD-LDLA 202
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-186 |
8.94e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 74.36 E-value: 8.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 1 MGMLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLrlltglsR-------PDAGEVLWQGQPLHQV--- 70
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLL-------RmiagfetPDSGRILLDGRDVTGLppe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 71 -RD------SYhqnLLWiGHqpgiktrLTALENLHFY--HRDGDTAQC----LEALAQAGLAGFEDIPVNQLSAGQQRRV 137
Cdd:COG3842 76 kRNvgmvfqDY---ALF-PH-------LTVAENVAFGlrMRGVPKAEIrarvAELLELVGLEGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9911057 138 ALARLWLTRATLWILDEPFTAIDVngvdRLTQRMAQ-----HTEQGGIVILTTH 186
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDA----KLREEMREelrrlQRELGITFIYVTH 194
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
21-186 |
1.19e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 72.65 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRdsyhqnllwiGHQPGIKT---------RL 91
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP----------PHKRPVNTvfqnyalfpHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 TALENLHFYHR----DGDT--AQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVngvd 165
Cdd:cd03300 88 TVFENIAFGLRlkklPKAEikERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL---- 163
|
170 180
....*....|....*....|....*.
gi 9911057 166 RLTQRM-----AQHTEQGGIVILTTH 186
Cdd:cd03300 164 KLRKDMqlelkRLQKELGITFVFVTH 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-193 |
1.22e-15 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 74.55 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCE--RDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDA---GEVLWQGQPLHQVRDSYHQ- 76
Cdd:COG1123 4 LLEVRDLSVRypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 77 -------------NLLWIGHQPGIktrltALENLHFyHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLW 143
Cdd:COG1123 84 rigmvfqdpmtqlNPVTVGDQIAE-----ALENLGL-SRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9911057 144 LTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGI-VILTTHQPLNVAE 193
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTtVLLITHDLGVVAE 208
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-187 |
1.30e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 13 RDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSY-HQNLLWIGHQPGIKTRl 91
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYlHRQVALVGQEPVLFSG- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 TALENLHFYHRDGDTAQCLEALAQAGLAGF-------EDIPV----NQLSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEIMAAAKAANAHDFimefpngYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180
....*....|....*....|....*..
gi 9911057 161 VNGVDRLTQRMAQhteQGGIVILTTHQ 187
Cdd:TIGR00958 650 AECEQLLQESRSR---ASRTVLLIAHR 673
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-188 |
2.18e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 71.36 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDA---GEVLWQGQPL-----HQVRDSY 74
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLtalpaEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 75 -HQNLLWIGHqpgiktrLTALENLHF-----YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRAT 148
Cdd:COG4136 81 lFQDDLLFPH-------LSVGENLAFalpptIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9911057 149 LWILDEPFTAIDVNgvdrLTQRM-----AQHTEQGGIVILTTHQP 188
Cdd:COG4136 154 ALLLDEPFSKLDAA----LRAQFrefvfEQIRQRGIPALLVTHDE 194
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-186 |
2.37e-15 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 71.13 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 13 RDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQ---VRDSYH--QNLlwiGHQPGI 87
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAkerRKSIGYvmQDV---DYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 88 KT-RLTALENLHFYHRDGDTAQCLeaLAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDR 166
Cdd:cd03226 87 DSvREELLLGLKELDAGNEQAETV--LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180
....*....|....*....|
gi 9911057 167 LTQRMAQHTEQGGIVILTTH 186
Cdd:cd03226 165 VGELIRELAAQGKAVIVITH 184
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
15-193 |
2.39e-15 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 71.35 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRD--SY-HQN--LL-Wighqpgik 88
Cdd:cd03293 16 AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPdrGYvFQQdaLLpW-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 89 trLTALEN------LHFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDV- 161
Cdd:cd03293 88 --LTVLDNvalgleLQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAl 165
|
170 180 190
....*....|....*....|....*....|....
gi 9911057 162 --NGVDRLTQRMAQHTEQGgiVILTTHqplNVAE 193
Cdd:cd03293 166 trEQLQEELLDIWRETGKT--VLLVTH---DIDE 194
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-192 |
2.66e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.11 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQvrdsyhqnllWIG 82
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAD----------WSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 83 HQPGiKTR------------LTALE--------NLHFYHRDGDTAQclEALAQAGLAGFEDIPVNQLSAGQQRRVALAR- 141
Cdd:PRK13548 72 AELA-RRRavlpqhsslsfpFTVEEvvamgrapHGLSRAEDDALVA--AALAQVDLAHLAGRDYPQLSGGEQQRVQLARv 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 142 ---LWL---TRATLwILDEPFTAIDV---NGVDRLTQRMAQhtEQGGIVILTTHQpLNVA 192
Cdd:PRK13548 149 laqLWEpdgPPRWL-LLDEPTSALDLahqHHVLRLARQLAH--ERGLAVIVVLHD-LNLA 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-156 |
3.06e-15 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 71.31 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDsyHQ-NLLWIG--HQ-PGIKTRLTALE 95
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP--HEiARLGIGrtFQiPRLFPELTVLE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9911057 96 NL----HFYHRDGDT------------AQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPF 156
Cdd:cd03219 95 NVmvaaQARTGSGLLlararreerearERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-193 |
3.95e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.06 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEwvqIT---GSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHqvRDSYHQnllwIGHQP-- 85
Cdd:COG4152 19 DVSFTVPKGE---IFgllGPNGAGK----------TttiriilgilAPDSGEVLWDGEPLD--PEDRRR----IGYLPee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 86 -GIKTRLTALENLHFYHR-DGDTAQclEALAQA-------GLAGFEDIPVNQLSAGQQRRVALArlwltrAT------LW 150
Cdd:COG4152 80 rGLYPKMKVGEQLVYLARlKGLSKA--EAKRRAdewlerlGLGDRANKKVEELSKGNQQKVQLI------AAllhdpeLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 9911057 151 ILDEPFTAID-VNgVDRLTQRMAQHTEQGGIVILTTHQpLNVAE 193
Cdd:COG4152 152 ILDEPFSGLDpVN-VELLKDVIRELAAKGTTVIFSSHQ-MELVE 193
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-186 |
4.05e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.96 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLhqvrDSYHQNLLWIG 82
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL----DYSKRGLLALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 83 HQpgIKTRLTALENLHFYHR-DGDTAQCL---------------EALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTR 146
Cdd:PRK13638 77 QQ--VATVFQDPEQQIFYTDiDSDIAFSLrnlgvpeaeitrrvdEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9911057 147 ATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTH 186
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSH 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-193 |
8.66e-15 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 70.26 E-value: 8.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 4 LEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQ-----PLHQvrdsyhQNL 78
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklPMHK------RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 79 LWIGH---QPGIKTRLTALENL------HFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATL 149
Cdd:cd03218 75 LGIGYlpqEASIFRKLTVEENIlavleiRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9911057 150 WILDEPFTAIDVNGVdRLTQRMAQHTEQGGIVILTT-HqplNVAE 193
Cdd:cd03218 155 LLLDEPFAGVDPIAV-QDIQKIIKILKDRGIGVLITdH---NVRE 195
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-186 |
8.89e-15 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 71.86 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEAREL-----LCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRdsyHQN 77
Cdd:COG1123 260 LLEVRNLskrypVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLS---RRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 78 LLWIGHQPGI---------KTRLTALENLHF---YHRDGDTAQC----LEALAQAGL-AGFEDIPVNQLSAGQQRRVALA 140
Cdd:COG1123 337 LRELRRRVQMvfqdpysslNPRMTVGDIIAEplrLHGLLSRAERrervAELLERVGLpPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 9911057 141 RLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGI-VILTTH 186
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLtYLFISH 463
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-186 |
1.29e-14 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 69.71 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 4 LEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGqpLHQVRDS--YHQNLLWI 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPreVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 82 GHQPGIKTRLTALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEP 155
Cdd:cd03265 79 FQDLSVDDELTGWENLYIharlygVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190
....*....|....*....|....*....|....
gi 9911057 156 FTAIDV---NGVDRLTQRMAQhtEQGGIVILTTH 186
Cdd:cd03265 159 TIGLDPqtrAHVWEYIEKLKE--EFGMTILLTTH 190
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
17-188 |
1.34e-14 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 69.77 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 17 TLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQ--------VRdSYH-----QNLLWIGH 83
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedararLR-ARHvgfvfQSFQLLPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 84 qpgiktrLTALEN----LHFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPfTAi 159
Cdd:COG4181 105 -------LTALENvmlpLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEP-TG- 175
|
170 180 190
....*....|....*....|....*....|....*
gi 9911057 160 dvnGVDRLT-QRMAQ-----HTEQGGIVILTTHQP 188
Cdd:COG4181 176 ---NLDAATgEQIIDllfelNRERGTTLVLVTHDP 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-188 |
1.38e-14 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 68.40 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQnllwighqpgiktrlta 93
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG----------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 94 lenlhfyhrdgdtaQCLEALAQAG--LAGfeDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRM 171
Cdd:cd03246 76 --------------DHVGYLPQDDelFSG--SIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170
....*....|....*..
gi 9911057 172 AQHTEQGGIVILTTHQP 188
Cdd:cd03246 140 AALKAAGATRIVIAHRP 156
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
17-186 |
1.57e-14 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 70.84 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 17 TLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLH----QVRD------SYhqnllwighqpG 86
Cdd:TIGR03265 18 TALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITrlppQKRDygivfqSY-----------A 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 87 IKTRLTALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:TIGR03265 87 LFPNLTVADNIAYglknrgMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALD 166
|
170 180
....*....|....*....|....*..
gi 9911057 161 VNGVDRLTQRMAQHTEQGGI-VILTTH 186
Cdd:TIGR03265 167 ARVREHLRTEIRQLQRRLGVtTIMVTH 193
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-188 |
1.67e-14 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 69.16 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQV-RDSYHQNLLWIGHQPgiktRL- 91
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLdPADLRRNIGYVPQDV----TLf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 --TALENLHFYHRDGDTAQCLEALAQAGLAGFE-------DIPVN----QLSAGQQRRVALARLWLTRATLWILDEPFTA 158
Cdd:cd03245 91 ygTLRDNITLGAPLADDERILRAAELAGVTDFVnkhpnglDLQIGergrGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190
....*....|....*....|....*....|
gi 9911057 159 IDVNGVDRLTQRMAQHTEqGGIVILTTHQP 188
Cdd:cd03245 171 MDMNSEERLKERLRQLLG-DKTLIIITHRP 199
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
15-187 |
1.73e-14 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 68.37 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIG---HQPGIKTRL 91
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGmvfQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 TALENLhfyhrdgdtaqcleALAqaglagfedipvnqLSAGQQRRVALARLWLTRATLWILDEPFTAIDV---NGVDRLT 168
Cdd:cd03229 92 TVLENI--------------ALG--------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPitrREVRALL 143
|
170
....*....|....*....
gi 9911057 169 QRMaqHTEQGGIVILTTHQ 187
Cdd:cd03229 144 KSL--QAQLGITVVLVTHD 160
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-186 |
2.04e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.22 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 4 LEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPlhqVRDSYHQNLLWIGH 83
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEP---VPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 84 QP---GIKTRLTALENLHFYHRD-GDTAQCLEALAQ-----AGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDE 154
Cdd:PRK13537 85 VPqfdNLDPDFTVRENLLVFGRYfGLSAAAARALVPpllefAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190
....*....|....*....|....*....|..
gi 9911057 155 PFTAIDVNGVDRLTQRMAQHTEQGGIVILTTH 186
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-186 |
2.81e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 13 RDERTLFSGLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQG------------------ 64
Cdd:COG0488 8 FGGRPLLDDVSLSINPGDRIGLVGRNGAGK----------StllkilagelEPDSGEVSIPKglrigylpqeppldddlt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 65 ---------QPLHQVRDSYHQNLLWIGHQPGIKTRLTALENlHFYHRDGDTA--QCLEALAQAGLAGFE-DIPVNQLSAG 132
Cdd:COG0488 78 vldtvldgdAELRALEAELEELEAKLAEPDEDLERLAELQE-EFEALGGWEAeaRAEEILSGLGFPEEDlDRPVSELSGG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9911057 133 QQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTeqgGIVILTTH 186
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP---GTVLVVSH 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
21-187 |
2.86e-14 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 68.33 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPL-------HQVRDSY-----HQNLLwighqpgik 88
Cdd:cd03262 18 GIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkkniNELRQKVgmvfqQFNLF--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 89 TRLTALENLHF-----YHRDGDTAQ--CLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDV 161
Cdd:cd03262 89 PHLTVLENITLapikvKGMSKAEAEerALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 168
|
170 180
....*....|....*....|....*.
gi 9911057 162 NGVDRLTQRMAQHTEQGGIVILTTHQ 187
Cdd:cd03262 169 ELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-193 |
3.10e-14 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 68.84 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 4 LEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQ-----PLHQvRDSyhqnl 78
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdithlPMHE-RAR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 79 LWIGH---QPGIKTRLTALENLH--FYHRDGDTAQCLEALAQAGLAGFE-----DIPVNQLSAGQQRRVALARLWLTRAT 148
Cdd:TIGR04406 76 LGIGYlpqEASIFRKLTVEENIMavLEIRKDLDRAEREERLEALLEEFQishlrDNKAMSLSGGERRRVEIARALATNPK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9911057 149 LWILDEPFTAIDVNGVDRLtQRMAQHTEQGGIVILTT-HqplNVAE 193
Cdd:TIGR04406 156 FILLDEPFAGVDPIAVGDI-KKIIKHLKERGIGVLITdH---NVRE 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-188 |
3.11e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 12 ERDERTLFSGLSFTLNAGEWVQITGSNGAGKTT--LLRLLTGLSRPDAGEV-LWQGQplhqvrdsyhqnllwighqpgIK 88
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTllRLLAGALKGTPVAGCVdVPDNQ---------------------FG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 89 TRLTALENLhfyHRDGDTAQCLEALAQAGLAgfeDI-----PVNQLSAGQQRRVALARLWLTRATLWILDEpFTAidvnG 163
Cdd:COG2401 98 REASLIDAI---GRKGDFKDAVELLNAVGLS---DAvlwlrRFKELSTGQKFRFRLALLLAERPKLLVIDE-FCS----H 166
|
170 180 190
....*....|....*....|....*....|...
gi 9911057 164 VDRLT--------QRMAQhtEQGGIVILTTHQP 188
Cdd:COG2401 167 LDRQTakrvarnlQKLAR--RAGITLVVATHHY 197
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-188 |
3.89e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 68.33 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 11 CERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGqplhqvRDSYhqnLLWIGHqpGIKTR 90
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSS---LLGLGG--GFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 LTALENLHFYHR-DGDTAQCLEALAQ-----AGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGV 164
Cdd:cd03220 99 LTGRENIYLNGRlLGLSRKEIDEKIDeiiefSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180
....*....|....*....|....
gi 9911057 165 DRLTQRMAQHTEQGGIVILTTHQP 188
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDP 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-186 |
4.09e-14 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 68.30 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNL--------LWighqpgikTRLT 92
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLgycpqfdaLF--------DELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 93 ALENLHFYHR------DGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTaidvnGVDR 166
Cdd:cd03263 92 VREHLRFYARlkglpkSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS-----GLDP 166
|
170 180
....*....|....*....|....
gi 9911057 167 LTQRM----AQHTEQGGIVILTTH 186
Cdd:cd03263 167 ASRRAiwdlILEVRKGRSIILTTH 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-207 |
4.27e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 67.90 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 22 LSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPL-------HQVRDSYHQNLLW----------IGHQ 84
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtaappadRPVSMLFQENNLFahltveqnvgLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 85 PGIKTRLTALENLHfyhrdgdtaqclEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGV 164
Cdd:cd03298 97 PGLKLTAEDRQAIE------------VALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 9911057 165 DRLTQRMAQ-HTEQGGIVILTTHQPLNVAESKIRRISLTQTRAA 207
Cdd:cd03298 165 AEMLDLVLDlHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-160 |
7.45e-14 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 68.05 E-value: 7.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 23 SFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDS------------YHQNLLWIGHqpgiktr 90
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrrkkismVFQSFALLPH------- 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9911057 91 LTALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:cd03294 117 RTVLENVAFglevqgVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-160 |
1.28e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 68.65 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQV-RDSYHQNLLWIGHQPGIKTRlT 92
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLtLESLRRQIGVVPQDTFLFSG-T 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9911057 93 ALENLHFYHRDGDTAQCLEALAQAGLAGF-------EDIPVNQ----LSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:COG1132 430 IRENIRYGRPDATDEEVEEAAKAAQAHEFiealpdgYDTVVGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALD 508
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-183 |
2.00e-13 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 66.99 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKTtllrlltglS---------RPDAGEVLWQGQPL-----HQV------RdSYhQNll 79
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKT---------TlfnlitgfyRPTSGRILFDGRDItglppHRIarlgiaR-TF-QN-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 80 wighqPGIKTRLTALENL----HFYHRDG-----------------DTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVA 138
Cdd:COG0411 88 -----PRLFPELTVLENVlvaaHARLGRGllaallrlprarreereARERAEELLERVGLADRADEPAGNLSYGQQRRLE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9911057 139 LARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVIL 183
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITIL 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-155 |
3.65e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWqGqplHQVRDSY-HQnllwi 81
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-G---ETVKIGYfDQ----- 385
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9911057 82 gHQPGIKTRLTALENLHFYHRDGDTAQCLEALAQAGLAGfEDI--PVNQLSAGQQRRVALARLWLTRATLWILDEP 155
Cdd:COG0488 386 -HQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSG-DDAfkPVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-186 |
4.37e-13 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 64.37 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHqvrdsyhqnllwighqpgIKTRLTALenlhfy 100
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------------------FASPRDAR------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 101 hrdgdtaqclealaQAGLAgfediPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGI 180
Cdd:cd03216 74 --------------RAGIA-----MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVA 134
|
....*.
gi 9911057 181 VILTTH 186
Cdd:cd03216 135 VIFISH 140
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-186 |
4.57e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 63.62 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWqgqplhqvrdsyHQNLLwIGHqpgiktrlta 93
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------------GSTVK-IGY---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 94 lenlhfyhrdgdtaqclealaqaglagfedipVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQ 173
Cdd:cd03221 68 --------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE 115
|
170
....*....|...
gi 9911057 174 HTeqgGIVILTTH 186
Cdd:cd03221 116 YP---GTVILVSH 125
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-187 |
5.34e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 1 MGMLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVlwqgqplhQVRDSYHQNLLW 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI--------RVGDITIDTARS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 81 IGHQPGIKTRL-----------------TALENL-------HFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRR 136
Cdd:PRK11264 73 LSQQKGLIRQLrqhvgfvfqnfnlfphrTVLENIiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9911057 137 VALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQ 187
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
20-199 |
9.21e-13 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 64.52 E-value: 9.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDS-------------YHQNLLWighqpg 86
Cdd:cd03258 22 KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkarrrigmifQHFNLLS------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 87 iktRLTALEN------LHFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:cd03258 96 ---SRTVFENvalpleIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9911057 161 VNGVDRLTQRMAQHTEQGGI-VILTTHQpLNVaeskIRRI 199
Cdd:cd03258 173 PETTQSILALLRDINRELGLtIVLITHE-MEV----VKRI 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
15-187 |
1.07e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.99 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQ-PGIKTRLT- 92
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQlRLLRTRLTm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 93 ------------ALEN--------LHFYHRDGDTaQCLEALAQAGLAGFEDI--PVNqLSAGQQRRVALARLWLTRATLW 150
Cdd:PRK10619 97 vfqhfnlwshmtVLENvmeapiqvLGLSKQEARE-RAVKYLAKVGIDERAQGkyPVH-LSGGQQQRVSIARALAMEPEVL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 9911057 151 ILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQ 187
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-186 |
1.23e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHQ--VRDSY-------HQNLLW 80
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGK----------StlmkilsgvyQPDSGEILLDGEPVRFrsPRDAQaagiaiiHQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 81 IGHqpgiktrLTALENL---HFYHRDG--DTAQcLEALAQAGLAGFE-----DIPVNQLSAGQQRRVALARLWLTRATLW 150
Cdd:COG1129 91 VPN-------LSVAENIflgREPRRGGliDWRA-MRRRARELLARLGldidpDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 9911057 151 ILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTH 186
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-186 |
1.30e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCER------DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVR-DSYH 75
Cdd:PRK10247 1 MQENSPLLQLQnvgylaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 76 QNLLWIGHQPGIKTRlTALENLHF-YHRDGDTAQclEALAQAGLAGFE------DIPVNQLSAGQQRRVALAR--LWLTR 146
Cdd:PRK10247 81 QQVSYCAQTPTLFGD-TVYDNLIFpWQIRNQQPD--PAIFLDDLERFAlpdtilTKNIAELSGGEKQRISLIRnlQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 9911057 147 ATLwiLDEPFTAIDVNG---VDRLTQRMAQhtEQGGIVILTTH 186
Cdd:PRK10247 158 VLL--LDEITSALDESNkhnVNEIIHRYVR--EQNIAVLWVTH 196
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-192 |
1.32e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.65 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRD-SYHQNLLWI 81
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 82 GHQP----GIKTR-LTALEN---LHFYHR--DGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWI 151
Cdd:PRK11231 82 PQHHltpeGITVReLVAYGRspwLSLWGRlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9911057 152 LDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQpLNVA 192
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD-LNQA 201
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-162 |
1.81e-12 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 63.64 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 13 RDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSY-HQNLLWIGHQPGIKTRl 91
Cdd:cd03248 24 RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlHSKVSLVGQEPVLFAR- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 TALENLHFYHRDGDTAQCLEALAQAGLAGFedIPV-------------NQLSAGQQRRVALARLWLTRATLWILDEPFTA 158
Cdd:cd03248 103 SLQDNIAYGLQSCSFECVKEAAQKAHAHSF--ISElasgydtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
....
gi 9911057 159 IDVN 162
Cdd:cd03248 181 LDAE 184
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
21-161 |
3.11e-12 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 63.29 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYhqnLLWIGHQPGI------------K 88
Cdd:cd03257 23 DVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRL---RKIRRKEIQMvfqdpmsslnprM 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9911057 89 TRLTALENLHFYHRDGDTAQCLEALAQAGLAGFEDIPV------NQLSAGQQRRVALARLWLTRATLWILDEPFTAIDV 161
Cdd:cd03257 100 TIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnrypHELSGGQRQRVAIARALALNPKLLIADEPTSALDV 178
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-187 |
3.12e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.48 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 4 LEAREL-LCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSrPDAGEVLWQGQPLHQV-RDSYHQNLLWI 81
Cdd:PRK11174 350 IEAEDLeILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELdPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 82 GHQPgiktRL---TALENLHFYHRDGDTAQCLEALAQAGLAGFE-------DIPVNQ----LSAGQQRRVALARLWLTRA 147
Cdd:PRK11174 429 GQNP----QLphgTLRDNVLLGNPDASDEQLQQALENAWVSEFLpllpqglDTPIGDqaagLSVGQAQRLALARALLQPC 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 9911057 148 TLWILDEPFTAIDVNGVDR----LTQRMAQHTeqggiVILTTHQ 187
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLvmqaLNAASRRQT-----TLMVTHQ 543
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
15-194 |
6.33e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.77 E-value: 6.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSyhqnllwighqpgikTRL--- 91
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED---------------TRLmfq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 --------TALENLHFYHRDGDTAQCLEALAQAGLAG-FEDIPVnQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVn 162
Cdd:PRK11247 89 darllpwkKVIDNVGLGLKGQWRDAALQALAAVGLADrANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALDA- 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 9911057 163 gvdrLTQRMAQH------TEQGGIVILTTHqplNVAES 194
Cdd:PRK11247 167 ----LTRIEMQDlieslwQQHGFTVLLVTH---DVSEA 197
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-186 |
9.36e-12 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 61.18 E-value: 9.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQPGIKTRlTAL 94
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 95 ENLhfyhrdgdtaqclealaqaGLagfedipvnQLSAGQQRRVALARLWLTRATLWILDEPftaidVNGVDRLTQR---- 170
Cdd:cd03247 93 NNL-------------------GR---------RFSGGERQRLALARILLQDAPIVLLDEP-----TVGLDPITERqlls 139
|
170
....*....|....*..
gi 9911057 171 -MAQHTEQGGIVILTTH 186
Cdd:cd03247 140 lIFEVLKDKTLIWITHH 156
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-183 |
9.61e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.31 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 6 ARELLCERDERTLFSGL------SFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPL-----HQ----- 69
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLlavnnvNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpgHQiarmg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 70 -VRDSYHQNLLwighqpgikTRLTALENL----HFYHRDGDTAQCL----------EALAQA-------GLAGFEDIPVN 127
Cdd:PRK11300 82 vVRTFQHVRLF---------REMTVIENLlvaqHQQLKTGLFSGLLktpafrraesEALDRAatwlervGLLEHANRQAG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9911057 128 QLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVIL 183
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVL 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-161 |
9.75e-12 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 61.86 E-value: 9.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQV-RDSYHQNLLWIGHQPGIKTRlTALENLHF 99
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsRKSLRSMIGVVLQDTFLFSG-TIMENIRL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9911057 100 YHRDGDTAQCLEALAQAGLA--------GFEDIPVNQ---LSAGQQRRVALARLWLTRATLWILDEPFTAIDV 161
Cdd:cd03254 100 GRPNATDEEVIEAAKEAGAHdfimklpnGYDTVLGENggnLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-186 |
1.01e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.93 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVrDSYHQNLLWIG 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-PPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 83 HQPGIKTRLTALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPF 156
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFglkqdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190
....*....|....*....|....*....|.
gi 9911057 157 TAIDVNGVDRLTQRMAQHTEQGGIV-ILTTH 186
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILERVGVTcVMVTH 208
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-186 |
1.05e-11 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 62.51 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 34 ITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVR------DSYHQNLLWIGHqpgiktrLTALENLHF------YH 101
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPphlrhiNMVFQSYALFPH-------MTVEENVAFglkmrkVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 102 RDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGI- 180
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIt 153
|
....*.
gi 9911057 181 VILTTH 186
Cdd:TIGR01187 154 FVFVTH 159
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-194 |
1.06e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.20 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQ--------PLHQVRDSYHQnllWIGHQPGIKTRLT 92
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvatldadALAQLRREHFG---FIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 93 ALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDR 166
Cdd:PRK10535 103 AAQNVEVpavyagLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
170 180
....*....|....*....|....*...
gi 9911057 167 LTQRMAQHTEQGGIVILTTHQPLNVAES 194
Cdd:PRK10535 183 VMAILHQLRDRGHTVIIVTHDPQVAAQA 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-186 |
1.13e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.74 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 23 SFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHqVRDSYHQNLLWIG--HQ-----P 85
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGK----------StlmkilyglyQPDSGEILIDGKPVR-IRSPRDAIALGIGmvHQhfmlvP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 86 giktRLTALENLHFYHRDG-----DTAQC---LEALAQAglAGFE---DIPVNQLSAGQQRRVALARLWLTRATLWILDE 154
Cdd:COG3845 94 ----NLTVAENIVLGLEPTkggrlDRKAArarIRELSER--YGLDvdpDAKVEDLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190
....*....|....*....|....*....|....*
gi 9911057 155 PfTAidV---NGVDRLTQRMAQHTEQGGIVILTTH 186
Cdd:COG3845 168 P-TA--VltpQEADELFEILRRLAAEGKSIIFITH 199
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-193 |
1.14e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.58 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 1 MGMLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQ----- 65
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGK----------TttfymivglvKPDSGRIFLDGEdithl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 66 PLHQ-VRdsyhqnlLWIGH---QPGIKTRLTALENL------HFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQR 135
Cdd:COG1137 71 PMHKrAR-------LGIGYlpqEASIFRKLTVEDNIlavlelRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9911057 136 RVALARLWLTRATLWILDEPFTAIDVNGVDRLtQRMAQHTEQGGI-VILTTHqplNVAE 193
Cdd:COG1137 144 RVEIARALATNPKFILLDEPFAGVDPIAVADI-QKIIRHLKERGIgVLITDH---NVRE 198
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-201 |
1.20e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.76 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 22 LSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDS-----YHQNLLWIGHQPGIKTRLTALEN 96
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelRNQKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 97 ----LHFYHRDGDTAQ--CLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQR 170
Cdd:PRK11629 108 vampLLIGKKKPAEINsrALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
|
170 180 190
....*....|....*....|....*....|.
gi 9911057 171 MAQHTEQGGIVILTTHQPLNVAESKIRRISL 201
Cdd:PRK11629 188 LGELNRLQGTAFLVVTHDLQLAKRMSRQLEM 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-187 |
1.37e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.65 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 17 TLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQ----PLHQVRDsYHQNLLWIGHQPGIKTRLT 92
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvndPKVDERL-IRQEAGMVFQQFYLFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 93 ALENLHF--YHRDGDT-----AQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVD 165
Cdd:PRK09493 94 ALENVMFgpLRVRGASkeeaeKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRH 173
|
170 180
....*....|....*....|..
gi 9911057 166 RLTQRMAQHTEQGGIVILTTHQ 187
Cdd:PRK09493 174 EVLKVMQDLAEEGMTMVIVTHE 195
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-186 |
1.46e-11 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 61.33 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQV---RDSYHQN---LLWighqpgiktrLTAL 94
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNyslLPW----------LTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 95 EN--------LHFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDR 166
Cdd:TIGR01184 73 ENialavdrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|.
gi 9911057 167 LTQRMAQHTEQGGI-VILTTH 186
Cdd:TIGR01184 153 LQEELMQIWEEHRVtVLMVTH 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-186 |
1.71e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.64 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLH---QVRDSYHQN-- 77
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERGVVFQNeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 78 -LLWighqpgiktrLTALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLW 150
Cdd:PRK11248 81 lLPW----------RNVQDNVAFglqlagVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 9911057 151 ILDEPFTAIDVNGVDRLTQRMAQ-HTEQGGIVILTTH 186
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKlWQETGKQVLLITH 187
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
14-160 |
1.73e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 62.27 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQ----------PLHQVRDSY----Hqnll 79
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenrHVNTVFQSYalfpH---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 80 wighqpgiktrLTALENLHFYHR------DGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILD 153
Cdd:PRK09452 101 -----------MTVFENVAFGLRmqktpaAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
....*..
gi 9911057 154 EPFTAID 160
Cdd:PRK09452 170 ESLSALD 176
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
12-188 |
3.04e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.60 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 12 ERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPD---AGEVLWQGQPLH----QVRDSY-HQNLLWIGH 83
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDakemRAISAYvQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 84 qpgiktrLTALENLHF-----YHRDGDTAQCLEA----LAQAGLAGFED----IP--VNQLSAGQQRRVALARLWLTRAT 148
Cdd:TIGR00955 114 -------LTVREHLMFqahlrMPRRVTKKEKRERvdevLQALGLRKCANtrigVPgrVKGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 9911057 149 LWILDEPFTAID---VNGVDRLTQRMAQhteQGGIVILTTHQP 188
Cdd:TIGR00955 187 LLFCDEPTSGLDsfmAYSVVQVLKGLAQ---KGKTIICTIHQP 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
111-162 |
4.77e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.89 E-value: 4.77e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 9911057 111 EALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVN 162
Cdd:PRK11432 119 EALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-186 |
6.19e-11 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 59.62 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 13 RDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQV-----RDSyhqnllwIGH---Q 84
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvelRRK-------IGYviqQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 85 PGIKTRLTALEN------LHFYHRDGDTAQCLEALAQAGL--AGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPF 156
Cdd:cd03295 84 IGLFPHMTVEENialvpkLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190
....*....|....*....|....*....|.
gi 9911057 157 TAIDVNGVDRLTQRMAQ-HTEQGGIVILTTH 186
Cdd:cd03295 164 GALDPITRDQLQEEFKRlQQELGKTIVFVTH 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-188 |
7.13e-11 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 59.21 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 12 ERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDA---GEVLWQGQPL--HQVRD--SY-HQNLLWIGH 83
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRkpDQFQKcvAYvRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 84 qpgiktrLTALENLHFY-----HRDGDTAQ-----CLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILD 153
Cdd:cd03234 96 -------LTVRETLTYTailrlPRKSSDAIrkkrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190
....*....|....*....|....*....|....*
gi 9911057 154 EPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQP 188
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQP 203
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-186 |
9.90e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.22 E-value: 9.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 19 FSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQpgiktRL-----TA 93
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQ-----RVhlfsaTL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 94 LENLHFYHRDGDTAQCLEALAQAGLAGF--EDIPVN--------QLSAGQQRRVALARLWLTRATLWILDEPftaidVNG 163
Cdd:PRK11160 431 RDNLLLAAPNASDEALIEVLQQVGLEKLleDDKGLNawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEP-----TEG 505
|
170 180
....*....|....*....|....*...
gi 9911057 164 VDRLTQR-----MAQHTeQGGIVILTTH 186
Cdd:PRK11160 506 LDAETERqilelLAEHA-QNKTVLMITH 532
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-188 |
1.20e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.82 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKttllrlltglS------------------RPDAGEVLWQGQ----PLHQVR 71
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGK----------StllraiaglwpygsgriaRPAGARVLFLPQrpylPLGTLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 72 D--SYhqnllwighqPGIktrltalenlhfyHRDGDTAQCLEALAQAGLAGFE---DIPVN---QLSAGQQRRVALARLW 143
Cdd:COG4178 444 EalLY----------PAT-------------AEAFSDAELREALEAVGLGHLAerlDEEADwdqVLSLGEQQRLAFARLL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9911057 144 LTRATLWILDEPFTAIDVNGVDRLTQRMaQHTEQGGIVILTTHQP 188
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLL-REELPGTTVISVGHRS 544
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-188 |
1.53e-10 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 57.95 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 4 LEARELLCERDE------RTLFSGLSFTLNAGEWVQITGSNGAGKTT--LLRLLTGLSRPDAGEVLWQGQPLHQVRDSYH 75
Cdd:cd03213 4 LSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTllNALAGRRTGLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 76 -----QNLLWIGHqpgiktrLTALENLHFyhrdgdtaqclealaQAGLAGfedipvnqLSAGQQRRVALARLWLTRATLW 150
Cdd:cd03213 84 igyvpQDDILHPT-------LTVRETLMF---------------AAKLRG--------LSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 9911057 151 ILDEP------FTAIDVNgvdRLTQRMAQhteQGGIVILTTHQP 188
Cdd:cd03213 134 FLDEPtsgldsSSALQVM---SLLRRLAD---TGRTIICSIHQP 171
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-186 |
1.96e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 58.11 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 2 GMLEARELLCERDERTL--FSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNll 79
Cdd:cd03267 18 GLIGSLKSLFKRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 80 wIGHQPGIKTRL----TALENLHFYHR-----DGDTAQCLEALAQA-GLAGFEDIPVNQLSAGQQRRVALARLWLTRATL 149
Cdd:cd03267 96 -IGVVFGQKTQLwwdlPVIDSFYLLAAiydlpPARFKKRLDELSELlDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 9911057 150 WILDEPFTAIDVNGVDRLTQRMAQHT-EQGGIVILTTH 186
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNrERGTTVLLTSH 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-194 |
2.59e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.98 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 1 MGMLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQ-----PLHQvrdSYH 75
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHA---RAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 76 QNLLWIGHQPGIKTRLTALENLH--FYHRDGDTAQ-----CLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRAT 148
Cdd:PRK10895 78 RGIGYLPQEASIFRRLSVYDNLMavLQIRDDLSAEqredrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9911057 149 LWILDEPFTAID-VNGVDrlTQRMAQHTEQGGI-VILTTHqplNVAES 194
Cdd:PRK10895 158 FILLDEPFAGVDpISVID--IKRIIEHLRDSGLgVLITDH---NVRET 200
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-155 |
3.86e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKttllrlltglSR---------PDA---GEVLWQGQPLH--QVRDS-------YHQNLL 79
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGK----------STlmkvlsgvyPHGtyeGEIIFEGEELQasNIRDTeragiaiIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 80 WIGHqpgiktrLTALENL---------HFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLW 150
Cdd:PRK13549 93 LVKE-------LSVLENIflgneitpgGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
....*
gi 9911057 151 ILDEP 155
Cdd:PRK13549 166 ILDEP 170
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-159 |
4.08e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.30 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLsRPDA---GEVLWQGQPL--HQVRDSYHQN 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLkaSNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 78 LLWIGHQPGIKTRLTALENLHF----------YHRDGDTAQCLEALAQAGLAGFED-IPVNQLSAGQQRRVALARLWLTR 146
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLgneitlpggrMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQ 159
|
170
....*....|...
gi 9911057 147 ATLWILDEPFTAI 159
Cdd:TIGR02633 160 ARLLILDEPSSSL 172
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
13-193 |
4.34e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 13 RDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPlhqVRDSYHQNLL-WIGHQPGIKTRL 91
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP---TRQALQKNLVaYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 TAL-ENLHFYHRDG-----------DTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAI 159
Cdd:PRK15056 94 PVLvEDVVMMGRYGhmgwlrrakkrDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190
....*....|....*....|....*....|....
gi 9911057 160 DVNGVDRLTQRMAQHTEQGGIVILTTHQPLNVAE 193
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNLGSVTE 207
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-186 |
5.12e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.40 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHQVRDsyHQNLLWIGH 83
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGK----------StllnaiagslPPDSGSILIDGKDVTKLPE--YKRAKYIGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 84 --Q-PGIKT--RLTALEN------------LHFYHRDGDTAQCLEALAQAGLaGFED---IPVNQLSAGQqrRVALARLW 143
Cdd:COG1101 85 vfQdPMMGTapSMTIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLGL-GLENrldTKVGLLSGGQ--RQALSLLM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9911057 144 --LTRATLWILDE------PFTAIDVNgvdRLTQRMAQhtEQGGIVILTTH 186
Cdd:COG1101 162 atLTKPKLLLLDEhtaaldPKTAALVL---ELTEKIVE--ENNLTTLMVTH 207
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-186 |
5.70e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.55 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELlCER--DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRD---SYHQN 77
Cdd:PRK13636 5 ILKVEEL-NYNysDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 78 LLWIGHQPGIKT-RLTALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLW 150
Cdd:PRK13636 84 VGMVFQDPDNQLfSASVYQDVSFgavnlkLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 9911057 151 ILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVIL-TTH 186
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIiATH 200
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-186 |
8.50e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 56.95 E-value: 8.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQ--VRDSYHQnllwIG---HQP--- 85
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVRRQ----VGmvfQNPdnq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 86 --GIKTR---LTALENlHFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:PRK13635 94 fvGATVQddvAFGLEN-IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180
....*....|....*....|....*..
gi 9911057 161 VNGVDRLTQRMAQHTEQGGI-VILTTH 186
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGItVLSITH 199
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-183 |
9.31e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 9.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLfSGLSFTLNAGEWVQITGSNGAGKttllrllTGLSRPDAGE-VLWQGQPLHQ----VRDSYHQ------------ 76
Cdd:PRK10938 15 DTKTL-QLPSLTLNAGDSWAFVGANGSGK-------SALARALAGElPLLSGERQSQfshiTRLSFEQlqklvsdewqrn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 77 --NLLWIGHQpgiKTRLTALENLHFYHRdgDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDE 154
Cdd:PRK10938 87 ntDMLSPGED---DTGRTTAEIIQDEVK--DPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180
....*....|....*....|....*....
gi 9911057 155 PFTAIDVNGVDRLTQRMAQHTEQGGIVIL 183
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
21-160 |
1.31e-09 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 55.81 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVrDSYHQNLLWIGHQPGIKTRLTALENLHFY 100
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV-PVQERNVGFVFQHYALFRHMTVFDNVAFG 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 101 HR----------DGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:cd03296 99 LRvkprserppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-186 |
1.36e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 56.28 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 11 CERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQvrdsyhQNLLWIGHQPGIKTR 90
Cdd:PRK13647 13 RYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA------ENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 --------LTALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPF 156
Cdd:PRK13647 87 dpddqvfsSTVWDDVAFgpvnmgLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190
....*....|....*....|....*....|
gi 9911057 157 TAIDVNGVDRLTQRMAQHTEQGGIVILTTH 186
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATH 196
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-163 |
1.65e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.89 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQgqplHQVRDSYHQNLLWIghQPGIKTRLTAL 94
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN----GKLRIGYVPQKLYL--DTTLPLTVNRF 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9911057 95 ENLHFYHRDGDTaqcLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNG 163
Cdd:PRK09544 90 LRLRPGTKKEDI---LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-183 |
1.71e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 54.75 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERdertLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHqvRDSYHQNL-LWI 81
Cdd:cd03215 4 VLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT--RRSPRDAIrAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 82 GHQP------GIKTRLTALENLhfyhrdgdtaqcleALAQaglagfedipvnQLSAGQQRRVALARlWLTR-ATLWILDE 154
Cdd:cd03215 78 AYVPedrkreGLVLDLSVAENI--------------ALSS------------LLSGGNQQKVVLAR-WLARdPRVLILDE 130
|
170 180
....*....|....*....|....*....
gi 9911057 155 PFTAIDVNGVDRLTQRMAQHTEQGGIVIL 183
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIRELADAGKAVLL 159
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-186 |
2.31e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 55.92 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPL---HQVRDSYhqnllw 80
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGK----------TtllriiagleTPDSGRIVLNGRDLftnLPPRERR------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 81 IG----------HqpgiktrLTALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWL 144
Cdd:COG1118 77 VGfvfqhyalfpH-------MTVAENIAFglrvrpPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 9911057 145 TRATLWILDEPFTAIDVngvdRLTQRMAQ-----HTEQGGIVILTTH 186
Cdd:COG1118 150 VEPEVLLLDEPFGALDA----KVRKELRRwlrrlHDELGGTTVFVTH 192
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-160 |
3.31e-09 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 54.85 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 12 ERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVrdsyhqNLLWIGHQPGIKTR- 90
Cdd:cd03249 12 SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL------NLRWLRSQIGLVSQe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 -----LTALENLHFYHRDGDTAQCLEALAQAGLAGF-EDIPVN----------QLSAGQQRRVALARLWLTRATLWILDE 154
Cdd:cd03249 86 pvlfdGTIAENIRYGKPDATDEEVEEAAKKANIHDFiMSLPDGydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDE 165
|
....*.
gi 9911057 155 PFTAID 160
Cdd:cd03249 166 ATSALD 171
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-201 |
3.42e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 17 TLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYH-----QNLLWIGHQPGIKTRL 91
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 TALENLHFY-----HRDGDT-AQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVD 165
Cdd:PRK10584 104 NALENVELPallrgESSRQSrNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 9911057 166 RLTQRM-AQHTEQGGIVILTTHQPLNVAESKiRRISL 201
Cdd:PRK10584 184 KIADLLfSLNREHGTTLILVTHDLQLAARCD-RRLRL 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-193 |
4.18e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.81 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 1 MGMLEARELLCE-RDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQP-----LHQVRDS- 73
Cdd:PRK13652 1 MHLIETRDLCYSySGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPitkenIREVRKFv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 74 --YHQNLLWIGHQPGIKTRLT------ALENLHFYHRdgdtaqCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLT 145
Cdd:PRK13652 81 glVFQNPDDQIFSPTVEQDIAfgpinlGLDEETVAHR------VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9911057 146 RATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGI-VILTTHQPLNVAE 193
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMtVIFSTHQLDLVPE 203
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-156 |
4.25e-09 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 54.36 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRdSYHQNLLWIGHQP---GIKTRLTALENL 97
Cdd:cd03224 18 GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP-PHERARAGIGYVPegrRIFPELTVEENL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9911057 98 H--FYHRDGDTAQclEALAQA-----GLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPF 156
Cdd:cd03224 97 LlgAYARRRAKRK--ARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-186 |
5.15e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.46 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSrPDAGEVLWQGQPLhqvrDSYHQNLL-----WIGHQpgiktrLTAL 94
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPL----SDWSAAELarhraYLSQQ------QSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 95 ENLHFYH----------RDGDTAQCLEALAQA-GLAGFEDIPVNQLSAGQQRRVALAR----LWLT---RATLWILDEPF 156
Cdd:COG4138 82 FAMPVFQylalhqpagaSSEAVEQLLAQLAEAlGLEDKLSRPLTQLSGGEWQRVRLAAvllqVWPTinpEGQLLLLDEPM 161
|
170 180 190
....*....|....*....|....*....|...
gi 9911057 157 TAIDV---NGVDRLTQRMAQhteQGGIVILTTH 186
Cdd:COG4138 162 NSLDVaqqAALDRLLRELCQ---QGITVVMSSH 191
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
21-155 |
5.71e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 54.22 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHQVRdSYHQNLLWIGHQP---GI 87
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGK----------TtllkaisgllPPRSGSIRFDGEDITGLP-PHRIARLGIGYVPegrRI 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9911057 88 KTRLTALENLH---FYHRDGDTAQclEALAQAG-----LAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEP 155
Cdd:COG0410 90 FPSLTVEENLLlgaYARRDRAEVR--ADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-192 |
5.93e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 16 RTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRD-SYHQNLLWIGHQ----PGIKTR 90
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSkAFARKVAYLPQQlpaaEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 -LTALENLHFYHRDG-----DTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDV-NG 163
Cdd:PRK10575 104 eLVAIGRYPWHGALGrfgaaDREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIaHQ 183
|
170 180 190
....*....|....*....|....*....|.
gi 9911057 164 VD--RLTQRMAQhtEQGGIVILTTHQpLNVA 192
Cdd:PRK10575 184 VDvlALVHRLSQ--ERGLTVIAVLHD-INMA 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-184 |
7.51e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 53.57 E-value: 7.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQ-----PLHQVRDSyhqnLLWIGHQPGIKTRlTALE 95
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRSS----LTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 96 NLHFYHRDGDtAQCLEAL--AQAGLagfedipvnQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNgVDRLTQRMAq 173
Cdd:cd03369 101 NLDPFDEYSD-EEIYGALrvSEGGL---------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA-TDALIQKTI- 168
|
170
....*....|.
gi 9911057 174 HTEQGGIVILT 184
Cdd:cd03369 169 REEFTNSTILT 179
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-160 |
8.62e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.00 E-value: 8.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQG--------QPLHQVRDSy 74
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrSRLYTVRKR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 75 hQNLLWighQPG-IKTRLTALENLHFYHRDGDT-------AQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTR 146
Cdd:PRK11831 86 -MSMLF---QSGaLFTDMNVFDNVAYPLREHTQlpapllhSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161
|
170
....*....|....
gi 9911057 147 ATLWILDEPFTAID 160
Cdd:PRK11831 162 PDLIMFDEPFVGQD 175
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-186 |
9.26e-09 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 53.49 E-value: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQ-----PLHQVRDSY-HQNLLWIGHqpgiktrLTA 93
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlPPEKRDISYvPQNYALFPH-------MTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 94 LENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRL 167
Cdd:cd03299 89 YKNIAYglkkrkVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180
....*....|....*....|
gi 9911057 168 TQRMAQ-HTEQGGIVILTTH 186
Cdd:cd03299 169 REELKKiRKEFGVTVLHVTH 188
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
123-186 |
1.12e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.17 E-value: 1.12e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9911057 123 DIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTeqgGIVILTTH 186
Cdd:TIGR03719 156 DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP---GTVVAVTH 216
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-155 |
1.21e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLW--QGQPLHQVRDSYHQnllwighqpgIKTRL 91
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWseNANIGYYAQDHAYD----------FENDL 399
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9911057 92 TALENLHFYHRDGDTAQCLEALAQAGLAGFEDI--PVNQLSAGQQRRVALARLWLTRATLWILDEP 155
Cdd:PRK15064 400 TLFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIkkSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
10-188 |
1.28e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.98 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 10 LCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTtllrlltglsrpdagevlwqgqplhqvrdSYHQNLLWIghqpgikt 89
Cdd:cd03227 2 IVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKS-----------------------------TILDAIGLA-------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 90 rlTALENLHFYHRDGDTAQCLEALAQAGLAGFedipVNQLSAGQQRRVALA---RLW-LTRATLWILDEPFTAIDVNGVD 165
Cdd:cd03227 45 --LGGAQSATRRRSGVKAGCIVAAVSAELIFT----RLQLSGGEKELSALAlilALAsLKPRPLYILDEIDRGLDPRDGQ 118
|
170 180
....*....|....*....|...
gi 9911057 166 RLTQRMAQHTEQGGIVILTTHQP 188
Cdd:cd03227 119 ALAEAILEHLVKGAQVIVITHLP 141
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-186 |
1.37e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.01 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 22 LSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSrPDAGEVLWQGQPLhqvrDSYHQNLL-----WIGHQPgiktrlTALEN 96
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPL----EAWSAAELarhraYLSQQQ------TPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 97 LHFYH----------RDGDTAQCLEALAQA-GLAGFEDIPVNQLSAGQQRRVALA----RLWLT---RATLWILDEPFTA 158
Cdd:PRK03695 84 MPVFQyltlhqpdktRTEAVASALNEVAEAlGLDDKLGRSVNQLSGGEWQRVRLAavvlQVWPDinpAGQLLLLDEPMNS 163
|
170 180 190
....*....|....*....|....*....|.
gi 9911057 159 IDV---NGVDRLTQRMAQhteQGGIVILTTH 186
Cdd:PRK03695 164 LDVaqqAALDRLLSELCQ---QGIAVVMSSH 191
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
12-194 |
1.39e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.20 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 12 ERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQvrdsyhQNLLWIGHQPGIKTR- 90
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE------ENVWDIRHKIGMVFQn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 --------------LTALENLHFYHRDGdTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPF 156
Cdd:PRK13650 90 pdnqfvgatveddvAFGLENKGIPHEEM-KERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 9911057 157 TAIDVNGVDRLTQRMAQHTEQGGI-VILTTHQPLNVAES 194
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDYQMtVISITHDLDEVALS 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-181 |
1.88e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.52 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 5 EARELLCERDERTLFSG------LSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSY-HQ- 76
Cdd:PRK15439 7 TAPPLLCARSISKQYSGvevlkgIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKaHQl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 77 NLLWIGHQPGIKTRLTALENLHF-YHRDGDTAQCLEAL-AQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDE 154
Cdd:PRK15439 87 GIYLVPQEPLLFPNLSVKENILFgLPKRQASMQKMKQLlAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180
....*....|....*....|....*...
gi 9911057 155 PFTAIDVNGVDRLTQRMAQHTEQG-GIV 181
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQGvGIV 194
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-187 |
2.03e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 52.71 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 22 LSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPD----------AGEVLWQGQPLHQVRDSYHQNLlWIGHQPGIKTRL 91
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellGRTVQREGRLARDIRKSRANTG-YIFQQFNLVNRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 TALENLHF--------------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFT 157
Cdd:PRK09984 102 SVLENVLIgalgstpfwrtcfsWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIA 181
|
170 180 190
....*....|....*....|....*....|.
gi 9911057 158 AIDVNGVDRLTQRMAQHTEQGGI-VILTTHQ 187
Cdd:PRK09984 182 SLDPESARIVMDTLRDINQNDGItVVVTLHQ 212
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
21-194 |
2.07e-08 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 52.53 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLhQVRDSYHQNLLWIGHQP---GIKTRLTALENL 97
Cdd:TIGR03410 18 GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI-TKLPPHERARAGIAYVPqgrEIFPRLTVEENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 98 hfyhRDGdtaqcLEALAQAGLAGFEDI----PVNQ---------LSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGV 164
Cdd:TIGR03410 97 ----LTG-----LAALPRRSRKIPDEIyelfPVLKemlgrrggdLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSII 167
|
170 180 190
....*....|....*....|....*....|
gi 9911057 165 DRLTQRMAQHTEQGGIVILTTHQPLNVAES 194
Cdd:TIGR03410 168 KDIGRVIRRLRAEGGMAILLVEQYLDFARE 197
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-186 |
2.18e-08 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 52.26 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVrDSYHQNLLWIGHQPGIKTRLTA 93
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL-PPKDRDIAMVFQNYALYPHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 94 LENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVngvdRL 167
Cdd:cd03301 90 YDNIAFglklrkVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA----KL 165
|
170 180
....*....|....*....|....
gi 9911057 168 TQRMAQ-----HTEQGGIVILTTH 186
Cdd:cd03301 166 RVQMRAelkrlQQRLGTTTIYVTH 189
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-187 |
2.44e-08 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 52.49 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQPGIKTRLTA 93
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 94 LENLHFYHRDGDTAQCLEALAQAGL--------AGFEDIPVNQ---LSAGQQRRVALARLWLTRATLWILDEPFTAIDVN 162
Cdd:cd03252 93 RDNIALADPGMSMERVIEAAKLAGAhdfiselpEGYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180
....*....|....*....|....*
gi 9911057 163 GvDRLTQRMAQHTEQGGIVILTTHQ 187
Cdd:cd03252 173 S-EHAIMRNMHDICAGRTVIIIAHR 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-186 |
2.86e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLH--QVRDSYHQNLLWIgHQ-----PgiktRLT 92
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAGVAII-YQelhlvP----EMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 93 ALENL---HFYHRDG---------DTAQCLEALAqaglagfEDI----PVNQLSAGQQRRVALARLWLTRATLWILDEPF 156
Cdd:PRK11288 96 VAENLylgQLPHKGGivnrrllnyEAREQLEHLG-------VDIdpdtPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190
....*....|....*....|....*....|
gi 9911057 157 TAIDVNGVDRLTQRMAQHTEQGGIVILTTH 186
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-160 |
3.67e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDaGEVLWQGQPLHQVRdsyHQNLLWIGHQ--------- 84
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLN---RRQLLPVRHRiqvvfqdpn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 85 PGIKTRLTAL----ENLHFYHRDGDTAQ----CLEALAQAGL--AGFEDIPvNQLSAGQQRRVALARLWLTRATLWILDE 154
Cdd:PRK15134 373 SSLNPRLNVLqiieEGLRVHQPTLSAAQreqqVIAVMEEVGLdpETRHRYP-AEFSGGQRQRIAIARALILKPSLIILDE 451
|
....*.
gi 9911057 155 PFTAID 160
Cdd:PRK15134 452 PTSSLD 457
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-193 |
3.75e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.14 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 22 LSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQplHQVRDSYHQNLLWIGHQPGI-----KTRL---TA 93
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGY--HITPETGNKNLKKLRKKVSLvfqfpEAQLfenTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 94 LENLHF------YHRDGDTAQCLEALAQAGLAgfEDI----PVnQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNG 163
Cdd:PRK13641 104 LKDVEFgpknfgFSEDEAKEKALKWLKKVGLS--EDLisksPF-ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190
....*....|....*....|....*....|
gi 9911057 164 VDRLTQRMAQHTEQGGIVILTTHQPLNVAE 193
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAE 210
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
10-188 |
3.89e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 50.62 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 10 LCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLrlltglsRPDAGevLWqgqPLHQVRDSYHQ--NLLWIGHQPgi 87
Cdd:cd03223 8 LATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF-------RALAG--LW---PWGSGRIGMPEgeDLLFLPQRP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 88 ktrltalenlhfYHRDGdtaqcleALAQAGLAGFEDIpvnqLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRL 167
Cdd:cd03223 74 ------------YLPLG-------TLREQLIYPWDDV----LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
170 180
....*....|....*....|.
gi 9911057 168 TQRMaqhTEQGGIVILTTHQP 188
Cdd:cd03223 131 YQLL---KELGITVISVGHRP 148
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
11-196 |
7.37e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.14 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 11 CERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQG------QPLHQVRdsyhqNLLWIGHQ 84
Cdd:PRK13644 10 SYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfSKLQGIR-----KLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 85 pGIKTRL---TALENLHFyhrdGDTAQCL----------EALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWI 151
Cdd:PRK13644 85 -NPETQFvgrTVEEDLAF----GPENLCLppieirkrvdRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 9911057 152 LDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTH--QPLNVAESKI 196
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHnlEELHDADRII 206
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-155 |
8.98e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 50.89 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQvRDSYHQNLLWIGHQ---PGIKTRLTALEN 96
Cdd:COG4674 27 NDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTG-LDEHEIARLGIGRKfqkPTVFEELTVFEN 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9911057 97 LH-------------FYHRDG-DTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEP 155
Cdd:COG4674 106 LElalkgdrgvfaslFARLTAeERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEP 178
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-201 |
9.24e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.98 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLT----GLSRPDA----GEVLWQGQPLHQV---R 71
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltGGGAPRGarvtGDVTLNGEPLAAIdapR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 72 DSYHQNLLWIGHQPGIKTRLTALENLHFY----------HRDGDTAQCleALAQAGLAGFEDIPVNQLSAGQQRRV---- 137
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYpharragaltHRDGEIAWQ--ALALAGATALVGRDVTTLSGGELARVqfar 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9911057 138 ALARLWLTRATL-----WILDEPFTAIDVNGVDRL---TQRMAQHTEQGGIVILttHQPlNVAESKIRRISL 201
Cdd:PRK13547 159 VLAQLWPPHDAAqppryLLLDEPTAALDLAHQHRLldtVRRLARDWNLGVLAIV--HDP-NLAARHADRIAM 227
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-161 |
9.34e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.01 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 22 LSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVlwqgqpLHQVRDSYHQNLLWIghQPGiktrlTALENLHF-- 99
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------KHSGRISFSSQFSWI--MPG-----TIKENIIFgv 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9911057 100 ------YHRDGDTAQCLEALAQagLAGFEDIPVNQ----LSAGQQRRVALARLWLTRATLWILDEPFTAIDV 161
Cdd:cd03291 123 sydeyrYKSVVKACQLEEDITK--FPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-188 |
1.05e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.47 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 13 RDERTLFSGLSFTLNAGEWVQITGSNGAGKTtllrlltglS---------RPDAGEVLWQGQ--PLhqvrdsyhqnllwI 81
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKS---------TllkliagilEPTSGRVEVNGRvsAL-------------L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 82 GHQPGIKTRLTALENLHFY-----HRDGDTAQCLEALAQ-AGLAGFEDIPVNQLSAGQQRR----VALArlwlTRATLWI 151
Cdd:COG1134 94 ELGAGFHPELTGRENIYLNgrllgLSRKEIDEKFDEIVEfAELGDFIDQPVKTYSSGMRARlafaVATA----VDPDILL 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 9911057 152 LDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQP 188
Cdd:COG1134 170 VDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSM 206
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-187 |
1.29e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.17 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 33 QIT---GSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQPGIKTRLTALENLHFYH----RDGD 105
Cdd:TIGR01257 957 QITaflGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAqlkgRSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 106 TAQC-LEA-LAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPftaidVNGVDRLTQR----MAQHTEQGG 179
Cdd:TIGR01257 1037 EAQLeMEAmLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP-----TSGVDPYSRRsiwdLLLKYRSGR 1111
|
....*...
gi 9911057 180 IVILTTHQ 187
Cdd:TIGR01257 1112 TIIMSTHH 1119
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-186 |
1.57e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.17 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 29 GEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQPGIKTRLTALENLHFYHR-DGDTA 107
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARlRGVPA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 108 QCLEALAQ-----AGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVI 182
Cdd:TIGR01257 2045 EEIEKVANwsiqsLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVV 2124
|
....
gi 9911057 183 LTTH 186
Cdd:TIGR01257 2125 LTSH 2128
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-186 |
2.06e-07 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 49.54 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 12 ERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGqplHQVRDSYHQNLLwigHQPGIKTRL 91
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG---HDVRDYTLASLR---RQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 TAL------ENLHFYHRDGDTAQCLEALAQAGLAGF-EDIPVN----------QLSAGQQRRVALARLWLTRATLWILDE 154
Cdd:cd03251 85 VFLfndtvaENIAYGRPGATREEVEEAARAANAHEFiMELPEGydtvigergvKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190
....*....|....*....|....*....|..
gi 9911057 155 PFTAIDvNGVDRLTQRMAQHTEQGGIVILTTH 186
Cdd:cd03251 165 ATSALD-TESERLVQAALERLMKNRTTFVIAH 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-161 |
2.24e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.68 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 22 LSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLwqgqplHQVRDSYHQNLLWIghQPGiktrlTALENLHF-- 99
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK------HSGRISFSPQTSWI--MPG-----TIKDNIIFgl 511
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9911057 100 ------YHRDGDTAQCLEALAQagLAGFEDIPVNQ----LSAGQQRRVALARLWLTRATLWILDEPFTAIDV 161
Cdd:TIGR01271 512 sydeyrYTSVIKACQLEEDIAL--FPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
9-160 |
2.77e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 49.69 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 9 LLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYH------------- 75
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkafrrdiqmvfqd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 76 --------QNLLWIGHQPgiktrltaLENLHFYHRDGDTAQCLEALAQAGLA-GFEDIPVNQLSAGQQRRVALARLWLTR 146
Cdd:PRK10419 98 sisavnprKTVREIIREP--------LRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVE 169
|
170
....*....|....
gi 9911057 147 ATLWILDEPFTAID 160
Cdd:PRK10419 170 PKLLILDEAVSNLD 183
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
21-141 |
4.17e-07 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 48.84 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHQVRDSYHQ------------NL 78
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGK----------StllrcinlleEPDSGTITVDGEDLTDSKKDINKlrrkvgmvfqqfNL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 79 lwIGHqpgiktrLTALENL-----HFYHRDGDTA--QCLEALAQAGLAGFEDIPVNQLSAGQQRRVALAR 141
Cdd:COG1126 89 --FPH-------LTVLENVtlapiKVKKMSKAEAeeRAMELLERVGLADKADAYPAQLSGGQQQRVAIAR 149
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-186 |
4.52e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 48.98 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQvrdsyhQNLLWIGHQPGIKTR--- 90
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD------DNFEKLRKHIGIVFQnpd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 ------------LTALENlHFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTA 158
Cdd:PRK13648 94 nqfvgsivkydvAFGLEN-HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180
....*....|....*....|....*....
gi 9911057 159 IDVNGVDRLTQRMAQHTEQGGIVILT-TH 186
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISiTH 201
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-203 |
5.88e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 48.88 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 6 ARELLCERDERTL-FSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDS-----YHQNLL 79
Cdd:PRK10070 30 SKEQILEKTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevRRKKIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 80 WIGHQPGIKTRLTALENLHFYHRDGDTA------QCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILD 153
Cdd:PRK10070 110 MVFQSFALMPHMTVLDNTAFGMELAGINaeerreKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9911057 154 EPFTAID----VNGVDRLTQRMAQHTEQggiVILTTHQpLNVAESKIRRISLTQ 203
Cdd:PRK10070 190 EAFSALDplirTEMQDELVKLQAKHQRT---IVFISHD-LDEAMRIGDRIAIMQ 239
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-188 |
7.02e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.72 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPD--AGEVLWQ-GQPLHQV--RDSY-HQNLLWIGHqpgik 88
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANnRKPTKQIlkRTGFvTQDDILYPH----- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 89 trLTALENLHF---------YHRDGDTAQCLEALAQAGLAGFEDIPVNQ-----LSAGQQRRVALARLWLTRATLWILDE 154
Cdd:PLN03211 155 --LTVRETLVFcsllrlpksLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190
....*....|....*....|....*....|....
gi 9911057 155 PFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQP 188
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQP 266
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
123-186 |
8.00e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 8.00e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9911057 123 DIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTeqgGIVILTTH 186
Cdd:PRK11819 158 DAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYP---GTVVAVTH 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-182 |
1.02e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 47.79 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 25 TLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWqgqPLHQVrdSYHQNLLWIGHQPGIKTRLTALENLHFYHRDG 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---ELDTV--SYKPQYIKADYEGTVRDLLSSITKDFYTHPYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 105 DTaqclEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNG---VDRLTQRMAQHTEQGGIV 181
Cdd:cd03237 96 KT----EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmASKVIRRFAENNEKTAFV 171
|
.
gi 9911057 182 I 182
Cdd:cd03237 172 V 172
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-177 |
1.04e-06 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVR-DSYHQNllwIGHQPGiKTRL- 91
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTlDSLRRA---IGVVPQ-DTVLf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 --TALENLHfYHRDGDTAQCLEALAQAglAGFEDIPVN--------------QLSAGQQRRVALARLWLTRATLWILDEP 155
Cdd:cd03253 88 ndTIGYNIR-YGRPDATDEEVIEAAKA--AQIHDKIMRfpdgydtivgerglKLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180
....*....|....*....|..
gi 9911057 156 FTAIDVngvdrltqrmaqHTEQ 177
Cdd:cd03253 165 TSALDT------------HTER 174
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-161 |
1.37e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.03 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQV-RDSYHQNLLWIGHQPGIKTRlTALENLH 98
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVtRASLRRNIAVVFQDAGLFNR-SIEDNIR 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9911057 99 FYHRDGDTAQCLEAL--AQA------GLAGFEDIP---VNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDV 161
Cdd:PRK13657 431 VGRPDATDEEMRAAAerAQAhdfierKPDGYDTVVgerGRQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-160 |
1.58e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 46.88 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 23 SFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQP-------------LHQVRDSY-H----QNLlWIGHQ 84
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtttppsrrpvsmLFQENNLFsHltvaQNI-GLGLN 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9911057 85 PGIKtrLTAlenlhfyhrdgDTAQCLEALA-QAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:PRK10771 98 PGLK--LNA-----------AQREKLHAIArQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-205 |
1.79e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.79 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 16 RTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSyhqnllwigHQPGIKTRLTALE 95
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNR---------EVPFLRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 96 NLHFYHRD--------------GDTAQCLEALAQAGL--AGFEDIPVN---QLSAGQQRRVALARLWLTRATLWILDEPF 156
Cdd:PRK10908 86 QDHHLLMDrtvydnvaipliiaGASGDDIRRRVSAALdkVGLLDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9911057 157 TAIDVNGVDRLTQRMAQHTEQGGIVILTTHQPLNVAESKIRRISLTQTR 205
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-161 |
2.01e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGL--SRP---DAGEVLWQGQPL-----HQVRDSYHQNLLWIGHQ 84
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpSPPvvyPSGDIRFHGESLlhaseQTLRGVRGNKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 85 P--------GIKTRLTALENLHFYHRD----GDTAQCLEALAQAGLAG-FEDIPvNQLSAGQQRRVALARLWLTRATLWI 151
Cdd:PRK15134 101 PmvslnplhTLEKQLYEVLSLHRGMRReaarGEILNCLDRVGIRQAAKrLTDYP-HQLSGGERQRVMIAMALLTRPELLI 179
|
170
....*....|
gi 9911057 152 LDEPFTAIDV 161
Cdd:PRK15134 180 ADEPTTALDV 189
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-183 |
2.16e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 23 SFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQV--RDSYHQNLLWI-------GHQPGIKTR--- 90
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspQDGLANGIVYIsedrkrdGLVLGMSVKenm 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 -LTALEnlHFYHRDGDTAQCLEALAQAGLAGFEDI-------PVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVN 162
Cdd:PRK10762 352 sLTALR--YFSRAGGSLKHADEQQAVSDFIRLFNIktpsmeqAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVG 429
|
170 180
....*....|....*....|.
gi 9911057 163 GVDRLTQRMAQHTEQGGIVIL 183
Cdd:PRK10762 430 AKKEIYQLINQFKAEGLSIIL 450
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-197 |
2.25e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.01 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 19 FSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQvrdsyhQNLLWIGHQPGIKTR-------- 90
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA------ENVWNLRRKIGMVFQnpdnqfvg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 LTALENLHF------YHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGV 164
Cdd:PRK13642 97 ATVEDDVAFgmenqgIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190
....*....|....*....|....*....|...
gi 9911057 165 DRLTQRMAQHTEQGGIVILTTHQPLNVAESKIR 197
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAASSDR 209
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
128-193 |
3.34e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.38 E-value: 3.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9911057 128 QLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQPLNVAE 193
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLE 241
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
129-199 |
3.94e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.23 E-value: 3.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9911057 129 LSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQPLNVAESKIRRI 199
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTI 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-161 |
4.04e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.55 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCerdeRTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLH--QVRDSYHQNllw 80
Cdd:COG1129 256 VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirSPRDAIRAG--- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 81 IGHQP------GIKTRLTALENLhfyhrdgdTAQCLEALAQAGL--------------------AGFEDIPVNQLSAGQQ 134
Cdd:COG1129 329 IAYVPedrkgeGLVLDLSIRENI--------TLASLDRLSRGGLldrrreralaeeyikrlrikTPSPEQPVGNLSGGNQ 400
|
170 180
....*....|....*....|....*...
gi 9911057 135 RRVALARlWL-TRATLWILDEPFTAIDV 161
Cdd:COG1129 401 QKVVLAK-WLaTDPKVLILDEPTRGIDV 427
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-162 |
4.59e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 46.47 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 4 LEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWqGQPLH-----QVRDSYHQNl 78
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlayvdQSRDALDPN- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 79 lwighqpgiKTRLTALENLHFYHRDGDTaqclEALAQAGLAGF------EDIPVNQLSAGQQRRVALARLWLTRATLWIL 152
Cdd:TIGR03719 401 ---------KTVWEEISGGLDIIKLGKR----EIPSRAYVGRFnfkgsdQQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
170
....*....|
gi 9911057 153 DEPFTAIDVN 162
Cdd:TIGR03719 468 DEPTNDLDVE 477
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
17-184 |
5.24e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 17 TLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQPgiktrltALEN 96
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNP-------LLYM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 97 LHFYhrDGDTAQCLEA-LAQAGLAGFEDI-PVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQH 174
Cdd:PLN03073 596 MRCF--PGVPEQKLRAhLGSFGVTGNLALqPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLF 673
|
170
....*....|
gi 9911057 175 teQGGIVILT 184
Cdd:PLN03073 674 --QGGVLMVS 681
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-161 |
6.51e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.73 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQ-----------------------------PLHQVR 71
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdllkadpeaqkllrqkiqivfqnpygslnPRKKVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 72 DSYHQNLLwighqpgIKTRLTALENlhfyhrdgdTAQCLEALAQAGL-AGFEDIPVNQLSAGQQRRVALARLWLTRATLW 150
Cdd:PRK11308 113 QILEEPLL-------INTSLSAAER---------REKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVV 176
|
170
....*....|.
gi 9911057 151 ILDEPFTAIDV 161
Cdd:PRK11308 177 VADEPVSALDV 187
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-182 |
1.05e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.47 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVR-DSYHQNLLWIGHQPGIKTRLTA 93
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSRLAVVSQTPFLFSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 94 lENLHFYHRDGdTAQCLEALAQagLAGF-EDI---------PVNQ----LSAGQQRRVALARLWLTRATLWILDEPFTAI 159
Cdd:PRK10789 407 -NNIALGRPDA-TQQEIEHVAR--LASVhDDIlrlpqgydtEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180
....*....|....*....|...
gi 9911057 160 DVNGVDRLTQRMAQHTEQGGIVI 182
Cdd:PRK10789 483 DGRTEHQILHNLRQWGEGRTVII 505
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-160 |
1.06e-05 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 44.48 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 4 LEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGK-----TTLLRLLTGLSRPDAGEVLWQGQPLHQVRDsyhqNL 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKstllrLLNRLNDLIPGAPDEGEVLLDGKDIYDLDV----DV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 79 LWIGHQPGI---KT---RLTALEN------LHFYHRDGDTAQCLE-ALAQAGLAGFEDIPVN--QLSAGQQRRVALARLW 143
Cdd:cd03260 77 LELRRRVGMvfqKPnpfPGSIYDNvayglrLHGIKLKEELDERVEeALRKAALWDEVKDRLHalGLSGGQQQRLCLARAL 156
|
170
....*....|....*..
gi 9911057 144 LTRATLWILDEPFTAID 160
Cdd:cd03260 157 ANEPEVLLLDEPTSALD 173
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
21-186 |
1.43e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 44.68 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHQV----RD------SY----Hq 76
Cdd:COG3839 21 DIDLDIEDGEFLVLLGPSGCGK----------StllrmiagleDPTSGEILIGGRDVTDLppkdRNiamvfqSYalypH- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 77 nllwighqpgiktrLTALENLHFY----HRDGDT--AQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLW 150
Cdd:COG3839 90 --------------MTVYENIAFPlklrKVPKAEidRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 9911057 151 ILDEPFTAIDVNGVDRLTQRMAQ-HTEQGGIVILTTH 186
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRlHRRLGTTTIYVTH 192
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-186 |
1.47e-05 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 44.02 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQ-----PLHQVRDSYH---QN-LLWIGhqpgiktrl 91
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdiskiGLHDLRSRISiipQDpVLFSG--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 92 TALENLHFYHRDGDtAQCLEALAQAGLAGF-------EDIPV----NQLSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:cd03244 93 TIRSNLDPFGEYSD-EELWQALERVGLKEFveslpggLDTVVeeggENLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180
....*....|....*....|....*.
gi 9911057 161 VNGvDRLTQRMAQHTEQGGIVILTTH 186
Cdd:cd03244 172 PET-DALIQKTIREAFKDCTVLTIAH 196
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-186 |
1.49e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.40 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 22 LSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYH-QNLLWIGHQPG-------------- 86
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRsQRIRMIFQDPStslnprqrisqild 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 87 ----IKTRLTALENlhfyhrdgdTAQCLEALAQAGL----AGFEDipvNQLSAGQQRRVALARLWLTRATLWILDEPFTA 158
Cdd:PRK15112 112 fplrLNTDLEPEQR---------EKQIIETLRQVGLlpdhASYYP---HMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190
....*....|....*....|....*....|
gi 9911057 159 IDVNGVDRLTQRMAQHTEQGGI--VILTTH 186
Cdd:PRK15112 180 LDMSMRSQLINLMLELQEKQGIsyIYVTQH 209
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
129-187 |
1.96e-05 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 43.61 E-value: 1.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 129 LSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQR-MAQHTEQGGIVILTTHQ 187
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLNNKTRILVTHQ 187
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-186 |
2.19e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 43.92 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVR-DSYHQNLLWI 81
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPsRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 82 GHQPGIKTRLTALENLHF----YHRDGDTAQCL----EALAQAGLAGFEDIPVNQLSAGQQRR--VALArlwLTRATLWI 151
Cdd:COG4604 81 RQENHINSRLTVRELVAFgrfpYSKGRLTAEDReiidEAIAYLDLEDLADRYLDELSGGQRQRafIAMV---LAQDTDYV 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 9911057 152 -LDEPFTAIDVN-GVD--RLTQRMAQhtEQGGIVILTTH 186
Cdd:COG4604 158 lLDEPLNNLDMKhSVQmmKLLRRLAD--ELGKTVVIVLH 194
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-186 |
2.42e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.92 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKttllrlltglS----------RPDAGEVLWQGQPLHQVRDSYHQNllwIGHQPGIKTR 90
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGK----------SttikmltgilVPTSGEVRVLGYVPFKRRKEFARR---IGVVFGQRSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 L----TALENLHFYHR-----DGDTAQCLEALAQA-GLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPfTaId 160
Cdd:COG4586 107 LwwdlPAIDSFRLLKAiyripDAEYKKRLDELVELlDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEP-T-I- 183
|
170 180 190
....*....|....*....|....*....|..
gi 9911057 161 vnGVDRLTQRM------AQHTEQGGIVILTTH 186
Cdd:COG4586 184 --GLDVVSKEAireflkEYNRERGTTILLTSH 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
125-192 |
2.46e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 43.88 E-value: 2.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9911057 125 PVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILtTHQPLNVA 192
Cdd:PRK14246 150 PASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIV-SHNPQQVA 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
111-192 |
2.56e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.88 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 111 EALAQAGLA--GFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQ-HTEQGGIVILTTHQ 187
Cdd:PRK13637 125 RAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElHKEYNMTIILVSHS 204
|
....*
gi 9911057 188 PLNVA 192
Cdd:PRK13637 205 MEDVA 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
22-160 |
2.91e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 43.46 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 22 LSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEV--------------LWQGQPLHQ----VRDSYHqnlLWigh 83
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdfsktpsDKAIRELRRnvgmVFQQYN---LW--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 84 qpgikTRLTALENL-------HFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPF 156
Cdd:PRK11124 95 -----PHLTVQQNLieapcrvLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
....
gi 9911057 157 TAID 160
Cdd:PRK11124 170 AALD 173
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-187 |
3.28e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 43.66 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLC---ERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGlSRPD--AGEVLWQGQPL--HQVRDSYH 75
Cdd:TIGR02633 257 ILEARNLTCwdvINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGkfEGNVFINGKPVdiRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 76 QNLLWI-------GHQP----GIKTRLTALENLHFYHRDGDTAQ---CLEALAQAGLAGFE-DIPVNQLSAGQQRRVALA 140
Cdd:TIGR02633 336 AGIAMVpedrkrhGIVPilgvGKNITLSVLKSFCFKMRIDAAAElqiIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLA 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 9911057 141 RLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQ 187
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSE 462
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
13-160 |
3.62e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 43.78 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 13 RDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLlwighqpgiktrlT 92
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQND-------------S 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 93 ALENLHFYH--RDGDTAQCLEALAQagLAGFEDIP-----------VNqLSAGQQRRVALARLWLTRATLWILDEPFTAI 159
Cdd:TIGR00957 715 LRENILFGKalNEKYYQQVLEACAL--LPDLEILPsgdrteigekgVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
.
gi 9911057 160 D 160
Cdd:TIGR00957 792 D 792
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
129-192 |
4.03e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 43.08 E-value: 4.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9911057 129 LSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQ-HTEQGGIVILTTHQPLNVA 192
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlHKEKGLTTVLVTHSMEDAA 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
128-160 |
4.35e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 43.15 E-value: 4.35e-05
10 20 30
....*....|....*....|....*....|...
gi 9911057 128 QLSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:PRK10851 136 QLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
129-187 |
9.82e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.66 E-value: 9.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 9911057 129 LSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQ 187
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQ 799
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-169 |
1.11e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.24 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 24 FTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEV----------LWQGQPLHQ---VRD--------------SYHQ 76
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivarLQQDPPRNVegtVYDfvaegieeqaeylkRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 77 NLLWIGHQPGIK-----TRLTA-LENLHFYHRDGDTAQCLEALaqaGLAGfeDIPVNQLSAGQQRRVALARLWLTRATLW 150
Cdd:PRK11147 104 ISHLVETDPSEKnlnelAKLQEqLDHHNLWQLENRINEVLAQL---GLDP--DAALSSLSGGWLRKAALGRALVSNPDVL 178
|
170
....*....|....*....
gi 9911057 151 ILDEPFTAIDVNGVDRLTQ 169
Cdd:PRK11147 179 LLDEPTNHLDIETIEWLEG 197
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
22-160 |
1.12e-04 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 41.54 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 22 LSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQ-------PLHQVRDSYHQNLLWIGHQPGIKTRLTAL 94
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkPSEKAIRLLRQKVGMVFQQYNLWPHLTVM 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9911057 95 ENL-------HFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:COG4161 101 ENLieapckvLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
125-186 |
1.20e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.24 E-value: 1.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9911057 125 PVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTeqgGIVILTTH 186
Cdd:PRK11147 437 PVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQ---GTVLLVSH 495
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-186 |
1.21e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 41.36 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 4 LEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLS--RPDAGEVLWQGQPLHQVRDSYHQNL-LW 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLgIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 81 IGHQ-----PGIKTRltalenlhFYHRDGDtaqclealaqaglAGFedipvnqlSAGQQRRVALARLWLTRATLWILDEP 155
Cdd:cd03217 81 LAFQyppeiPGVKNA--------DFLRYVN-------------EGF--------SGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190
....*....|....*....|....*....|.
gi 9911057 156 FTAIDVNGVDRLTQRMAQHTEQGGIVILTTH 186
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
111-193 |
1.25e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 41.65 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 111 EALAQAGLAG--FEDIPVnQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQP 188
Cdd:PRK13649 127 EKLALVGISEslFEKNPF-ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLM 205
|
....*
gi 9911057 189 LNVAE 193
Cdd:PRK13649 206 DDVAN 210
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-167 |
1.39e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTT-------------LLRLLTGLSRPDAGEVLWQ-GQPLHQVRDSYHQ--- 76
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTllslitgdhpqgySNDLTLFGRRRGSGETIWDiKKHIGYVSSSLHLdyr 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 77 ------NLLWIGHQPGI--------KTRLTALENLHFYHRDGDTAqclealaqaglagfeDIPVNQLSAGQQRRVALARL 142
Cdd:PRK10938 351 vstsvrNVILSGFFDSIgiyqavsdRQQKLAQQWLDILGIDKRTA---------------DAPFHSLSWGQQRLALIVRA 415
|
170 180
....*....|....*....|....*
gi 9911057 143 WLTRATLWILDEPFTAIDvnGVDRL 167
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLD--PLNRQ 438
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-161 |
2.22e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 41.23 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPL-----HQVRDSyHQNLLWIGHQP--GIKTRLTA 93
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkdDEWRAV-RSDIQMIFQDPlaSLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 94 ----LENLHFYHRDGDTAQCLE----ALAQAGLagfedIP--VN----QLSAGQQRRVALARLWLTRATLWILDEPFTAI 159
Cdd:PRK15079 118 geiiAEPLRTYHPKLSRQEVKDrvkaMMLKVGL-----LPnlINryphEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
..
gi 9911057 160 DV 161
Cdd:PRK15079 193 DV 194
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
128-196 |
2.29e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 41.15 E-value: 2.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9911057 128 QLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVD---RLTQRMaqHTEQGGIVILTTH---QPLNVAESKI 196
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERL--NKEYKKRIIMVTHnmdQVLRIADEVI 222
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
124-189 |
2.45e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 2.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9911057 124 IPVNQLSAGQQRRVAL-ARLWLTR--ATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQPL 189
Cdd:pfam13304 232 LPAFELSDGTKRLLALlAALLSALpkGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
39-161 |
3.10e-04 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 40.85 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 39 GAGKTTLLRLLTGLSRPDAGEV-----LWQGQ------PLHQVRdsyhqnllwIG----------HqpgiktrLTALENL 97
Cdd:COG4148 35 GSGKTTLLRAIAGLERPDSGRIrlggeVLQDSargiflPPHRRR---------IGyvfqearlfpH-------LSVRGNL 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9911057 98 HFYHRDGDTAQCLEALAQA----GLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDV 161
Cdd:COG4148 99 LYGRKRAPRAERRISFDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-186 |
3.36e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 4 LEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSrPDAGEVLWQGQPLHQVRDSYHQNllwIG- 82
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAGRRPWRF*TWCANRRALRRT---IG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 83 HQP---GIKTRLTALENLHFYHRDGD------TAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILD 153
Cdd:NF000106 90 HRPvr*GRRESFSGRENLYMIGR*LDlsrkdaRARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190
....*....|....*....|....*....|...
gi 9911057 154 EPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTH 186
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQ 202
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-186 |
3.61e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 40.45 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 4 LEARELLCERDeRTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPD----AGEVLWQGQPLH--QVRD----S 73
Cdd:PRK10418 5 IELRNIALQAA-QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVApcALRGrkiaT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 74 YHQNLLwIGHQPGIKTRLTALENLHFYHRDGDTAQCLEALAQAGLAGFEDIPVN---QLSAGQQRRVALARLWLTRATLW 150
Cdd:PRK10418 84 IMQNPR-SAFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 9911057 151 ILDEPFTAIDVNGVDR---LTQRMAQhtEQGGIVILTTH 186
Cdd:PRK10418 163 IADEPTTDLDVVAQARildLLESIVQ--KRALGMLLVTH 199
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
111-193 |
3.69e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 40.49 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 111 EALAQAGLAG--FEDIPVnQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQP 188
Cdd:PRK13643 126 EKLEMVGLADefWEKSPF-ELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLM 204
|
....*
gi 9911057 189 LNVAE 193
Cdd:PRK13643 205 DDVAD 209
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
123-183 |
3.91e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.68 E-value: 3.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9911057 123 DIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVIL 183
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIV 460
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
113-184 |
4.69e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.15 E-value: 4.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9911057 113 LAQAGLAgfedipvnqLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILT 184
Cdd:PRK14243 145 LKQSGLS---------LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT 207
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
111-193 |
4.84e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 40.17 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 111 EALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQPLN 190
Cdd:PRK13640 126 DVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID 205
|
...
gi 9911057 191 VAE 193
Cdd:PRK13640 206 EAN 208
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
129-187 |
5.30e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 39.62 E-value: 5.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9911057 129 LSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQR--MAQHTEQGGIVILTTHQ 187
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHK 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-159 |
5.91e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.99 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLH--QVRDS-------YHQNLLWIGHqpgiktr 90
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSqeagigiIHQELNLIPQ------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 LTALENL----HFYHRDG--------DTAQCLeaLAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTA 158
Cdd:PRK10762 94 LTIAENIflgrEFVNRFGridwkkmyAEADKL--LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
.
gi 9911057 159 I 159
Cdd:PRK10762 172 L 172
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-192 |
7.05e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 39.58 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 15 ERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQ----PGIKTR 90
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQnattPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 LTALENLHFYH-------RDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNG 163
Cdd:PRK10253 99 QELVARGRYPHqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180
....*....|....*....|....*....
gi 9911057 164 VDRLTQRMAQHTEQGGIVILTTHQPLNVA 192
Cdd:PRK10253 179 QIDLLELLSELNREKGYTLAAVLHDLNQA 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-187 |
8.07e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.96 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQPGIKTRLTALENLHFY 100
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 101 --HRDGDTAQCLEAlaqaglAGFEDIPVN--------------QLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNgV 164
Cdd:PLN03232 1334 seHNDADLWEALER------AHIKDVIDRnpfgldaevseggeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVR-T 1406
|
170 180
....*....|....*....|...
gi 9911057 165 DRLTQRMAQHTEQGGIVILTTHQ 187
Cdd:PLN03232 1407 DSLIQRTIREEFKSCTMLVIAHR 1429
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-192 |
9.34e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 39.14 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 3 MLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPlHQVRDSY-------- 74
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-GQLRDLYalseaerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 75 ----------HQNL---LWIGHQPG--IKTRLTALENLHfYHRDGDTAQCLEALAQAGLAGFEDIPvNQLSAGQQRRVAL 139
Cdd:PRK11701 85 rllrtewgfvHQHPrdgLRMQVSAGgnIGERLMAVGARH-YGDIRATAGDWLERVEIDAARIDDLP-TTFSGGMQQRLQI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9911057 140 ARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHT-EQGGIVILTTHQpLNVA 192
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVrELGLAVVIVTHD-LAVA 215
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
91-186 |
9.44e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 LTALENLHFYHRDGDTAQCLEALAQAGLagfEDIPVNQ----LSAGQQRRVALARLWLTRA---TLWILDEPFTAIDVNG 163
Cdd:TIGR00630 791 MTVEEAYEFFEAVPSISRKLQTLCDVGL---GYIRLGQpattLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDD 867
|
90 100
....*....|....*....|...
gi 9911057 164 VDRLTQRMAQHTEQGGIVILTTH 186
Cdd:TIGR00630 868 IKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
110-187 |
9.63e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 110 LEA-LAQAGlAGFE----DIPVNqLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILT 184
Cdd:PTZ00243 761 LEAdLAQLG-GGLEteigEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLA 838
|
...
gi 9911057 185 THQ 187
Cdd:PTZ00243 839 THQ 841
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
111-186 |
9.86e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 38.92 E-value: 9.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9911057 111 EALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGI-VILTTH 186
Cdd:PRK13633 127 ESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGItIILITH 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-183 |
1.15e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 39.26 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 19 FSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQ--VRDSYHQNLLWIG---HQPG------I 87
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlsTAQRLARGLVYLPedrQSSGlyldapL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 88 KTRLTAL--ENLHFYHRDGDTAQCLEALAQAGLAGFEDI--PVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDV-- 161
Cdd:PRK15439 359 AWNVCALthNRRGFWIKPARENAVLERYRRALNIKFNHAeqAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVsa 438
|
170 180
....*....|....*....|...
gi 9911057 162 -NGVDRLTQRMAQhteQGGIVIL 183
Cdd:PRK15439 439 rNDIYQLIRSIAA---QNVAVLF 458
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
125-188 |
1.21e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.94 E-value: 1.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9911057 125 PVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQG-GIVILTTHQP 188
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDkGIIIISSEMP 452
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
91-186 |
1.27e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 91 LTALENLHFYHRDGDTAQCLEALAQAGLAGFE-DIPVNQLSAGQQRRVALARLWLT---RATLWILDEPFTAIDVNGVDR 166
Cdd:PRK00635 771 MTAYEAEKFFLDEPSIHEKIHALCSLGLDYLPlGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKA 850
|
90 100
....*....|....*....|
gi 9911057 167 LTQRMAQHTEQGGIVILTTH 186
Cdd:PRK00635 851 LIYVLQSLTHQGHTVVIIEH 870
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
129-188 |
1.32e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 38.96 E-value: 1.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9911057 129 LSAGQQRRVALARLWLTRATLWILDEPFTAIDVNgvdrLTQRMAQHTEQGGIVILT-THQP 188
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD----VEGYMYRLCREFGITLFSvSHRK 639
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
129-160 |
1.35e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 38.60 E-value: 1.35e-03
10 20 30
....*....|....*....|....*....|..
gi 9911057 129 LSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
129-182 |
1.67e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 37.94 E-value: 1.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 9911057 129 LSAGQQRRVALARLWLTRATLWILDEPFTAIDVN---GVDRLTQRMAQHTEQGGIVI 182
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIRRLSEEGKKTALVV 128
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-154 |
1.78e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 38.63 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 22 LSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLH-QVRDSYHQnllwighqpgiktrltalenlHF- 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTaDNREAYRQ---------------------LFs 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9911057 100 -----YH---------RDGDTAQCLEALAQAGLAG---FED--IPVNQLSAGQQRRVALARLWLTRATLWILDE 154
Cdd:COG4615 410 avfsdFHlfdrllgldGEADPARARELLERLELDHkvsVEDgrFSTTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-199 |
2.13e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 38.23 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQV--RDSYHQNLLWIGHQPGIKTRLTALENL 97
Cdd:PRK09700 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdhKLAAQLGIGIIYQELSVIDELTVLENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 98 HF---------------YHRDGDTAQCLeaLAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVN 162
Cdd:PRK09700 102 YIgrhltkkvcgvniidWREMRVRAAMM--LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 9911057 163 GVDRLTQRMAQHTEQGGIVILTTHQplnVAEskIRRI 199
Cdd:PRK09700 180 EVDYLFLIMNQLRKEGTAIVYISHK---LAE--IRRI 211
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-160 |
2.20e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 37.63 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 12 ERDERTLFSGLSFTLNAGEWVQITGSNGAGKTT----LLRLLTGLSRPDaGEVLWQGQPLHQVRDSYHQNLLWIG----H 83
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKEFAEKYPGEIIYVSeedvH 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9911057 84 QPgiktRLTALENLHFyhrdgdTAQCleaLAQAGLAGFedipvnqlSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:cd03233 95 FP----TLTVRETLDF------ALRC---KGNEFVRGI--------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-60 |
2.57e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.18 E-value: 2.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEV 60
Cdd:PRK11819 335 GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
128-192 |
2.59e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 37.84 E-value: 2.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9911057 128 QLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQ-HTEQGGIVILTTHQPLNVA 192
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENKTIILVSHDMNEVA 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
123-192 |
2.92e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 37.51 E-value: 2.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 123 DIPVNqLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIViLTTHQPLNVA 192
Cdd:PRK14267 145 DYPSN-LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIV-LVTHSPAQAA 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-182 |
2.97e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 37.87 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 25 TLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQ------------------GQPLHQVRDSYHQNLLWighqPG 86
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyikpdydgtvEDLLRSITDDLGSSYYK----SE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 87 IKTRLtALENLHfyhrdgdtaqclealaqaglagfeDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVN---G 163
Cdd:PRK13409 437 IIKPL-QLERLL------------------------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlA 491
|
170
....*....|....*....
gi 9911057 164 VDRLTQRMAQHTEQGGIVI 182
Cdd:PRK13409 492 VAKAIRRIAEEREATALVV 510
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-162 |
3.13e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.09 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 56 DAGEVLWQGQPL--HQVRDSyhQNLLWIGHQPGIKTRLTALENLHFYHRDGDTAQCLEALAQAGLAGF-EDIPvNQ---- 128
Cdd:PTZ00265 1275 NSGKILLDGVDIcdYNLKDL--RNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFiESLP-NKydtn 1351
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 9911057 129 -------LSAGQQRRVALARLWLTRATLWILDEPFTAIDVN 162
Cdd:PTZ00265 1352 vgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-170 |
3.21e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 37.78 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 13 RDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQPGIKTRLT 92
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 93 ALENLHFyHRDGDTAQCLEALAQAGLAGF-EDIPV----------NQLSAGQQRRVALARLWLTRATLWILDEPFTAIDv 161
Cdd:PRK10790 431 FLANVTL-GRDISEEQVWQALETVQLAELaRSLPDglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANID- 508
|
....*....
gi 9911057 162 NGVDRLTQR 170
Cdd:PRK10790 509 SGTEQAIQQ 517
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-186 |
3.49e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 37.56 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 20 SGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQplhqvrdsyhQNLLWIGhqPGIKTRLTALENLHF 99
Cdd:PRK13545 41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----------AALIAIS--SGLNGQLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 100 YH-RDGDTAQCLEALAQ-----AGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQ 173
Cdd:PRK13545 109 KGlMMGLTKEKIKEIIPeiiefADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE 188
|
170
....*....|...
gi 9911057 174 HTEQGGIVILTTH 186
Cdd:PRK13545 189 FKEQGKTIFFISH 201
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-186 |
4.24e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 37.28 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 14 DERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQ-P-----GI 87
Cdd:PRK13632 20 SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQnPdnqfiGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 88 ktrlTA-------LENlHFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAID 160
Cdd:PRK13632 100 ----TVeddiafgLEN-KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
170 180
....*....|....*....|....*..
gi 9911057 161 VNGVDRLTQRMAQHTEQGG-IVILTTH 186
Cdd:PRK13632 175 PKGKREIKKIMVDLRKTRKkTLISITH 201
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-160 |
5.23e-03 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 37.09 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 21 GLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVL------W----QGQPLHQVRDSYHQNLLwigHQP-GIKT 89
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdeWvdmtKPGPDGRGRAKRYIGIL---HQEyDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 90 RLTALENLhfyhrdgDTAQCLE---------ALAQAGLAGFED---------IPvNQLSAGQQRRVALARLWLTRATLWI 151
Cdd:TIGR03269 379 HRTVLDNL-------TEAIGLElpdelarmkAVITLKMVGFDEekaeeildkYP-DELSEGERHRVALAQVLIKEPRIVI 450
|
....*....
gi 9911057 152 LDEPFTAID 160
Cdd:TIGR03269 451 LDEPTGTMD 459
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
123-192 |
5.51e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 36.81 E-value: 5.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 123 DIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIViLTTHQPLNVA 192
Cdd:PRK14247 141 DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIV-LVTHFPQQAA 209
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-155 |
6.84e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 36.40 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 1 MGMLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDS--YHQNL 78
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9911057 79 LWIGHQPGIKTRLTALENLHFYHRDGDTAQCLEALAQAglagFEDIP---------VNQLSAGQQRRVALARLWLTRATL 149
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWV----YELFPrlherriqrAGTMSGGEQQMLAIGRALMSQPRL 158
|
....*.
gi 9911057 150 WILDEP 155
Cdd:PRK11614 159 LLLDEP 164
|
|
| |
